CYP17A1

{{Short description|Mammalian protein found in Homo sapiens}} {{cs1 config|name-list-style=vanc|display-authors=6}} {{Infobox enzyme |name=Steroid 17-alpha-hydroxylase/17,20 lyase |AltNames={{wikidata|properties|P2561}}, {{wikidata|aliases}}   |image= |image_size= |caption= |EC_number={{wikidata|property|P591}} |CAS_number={{wikidata|property|P231}} |GO_code = }}{{Infobox gene}}'''Cytochrome P450 17A1''' ('''steroid 17α-monooxygenase''', '''17α-hydroxylase''', '''17-alpha-hydroxylase''', '''17,20-lyase''', '''17,20-desmolase''') is an enzyme of the hydroxylase type that in humans is encoded by the ''CYP17A1'' gene on chromosome 10.<ref name=":0" /> It is ubiquitously expressed in many tissues and cell types, including the zona reticularis and zona fasciculata (but not zona glomerulosa) of the adrenal cortex as well as gonadal tissues.<ref>{{cite web |title=BioGPS - your Gene Portal System |url=http://biogps.org/#goto=genereport&id=1586 |url-status=live |archive-url=https://web.archive.org/web/20110820062552/http://biogps.org/#goto=genereport&id=1586 |archive-date=2011-08-20 |access-date=2016-10-11 |website=biogps.org}}</ref><ref name="isbn1-4160-2328-3" /> It has both 17α-hydroxylase and 17,20-lyase activities, and is a key enzyme in the steroidogenic pathway that produces progestins, mineralocorticoids, glucocorticoids, androgens, and estrogens. More specifically, the enzyme acts upon pregnenolone and progesterone to add a hydroxyl (-OH) group at carbon 17 position (C17) of the steroid D ring (the 17α-hydroxylase activity, {{EC number|1.14.14.19}}), or acts upon 17α-hydroxyprogesterone and 17α-hydroxypregnenolone to split the side-chain off the steroid nucleus (the 17,20-lyase activity, {{EC number|1.14.14.32}}).<ref name="isbn1-4160-2328-3">{{cite book |author=Boulpaep EL |title=Medical physiology: a cellular and molecular approach |author2=Boron, WF |publisher=Elsevier Saunders |year=2005 |isbn=1-4160-2328-3 |location=St. Louis, Mo |page=1180}}</ref>

== Structure ==

===Gene=== The ''CYP17A1'' gene resides on chromosome 10 at the band 10q24.3 and contains 8 exons.<ref name=":0" /> The cDNA of this gene spans a length of 1527 bp.<ref name=":1">{{cite journal |vauthors=Vasaitis TS, Bruno RD, Njar VC |date=May 2011 |title=CYP17 inhibitors for prostate cancer therapy |journal=The Journal of Steroid Biochemistry and Molecular Biology |volume=125 |issue=1–2 |pages=23–31 |doi=10.1016/j.jsbmb.2010.11.005 |pmc=3047603 |pmid=21092758}}</ref> This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are generally regarded as monooxygenases that catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, and other lipids, including the remarkable carbon-carbon bond scission catalyzed by this enzyme.{{cn|date=January 2026}}

The ''CYP17A1'' gene may also contain variants associated with increased risk of coronary artery disease.<ref name="ReferenceA">{{cite journal |vauthors=Mega JL, Stitziel NO, Smith JG, Chasman DI, Caulfield M, Devlin JJ, Nordio F, Hyde C, Cannon CP, Sacks F, Poulter N, Sever P, Ridker PM, Braunwald E, Melander O, Kathiresan S, Sabatine MS |date=June 2015 |title=Genetic risk, coronary heart disease events, and the clinical benefit of statin therapy: an analysis of primary and secondary prevention trials |journal=Lancet |volume=385 |issue=9984 |pages=2264–2271 |doi=10.1016/S0140-6736(14)61730-X |pmc=4608367 |pmid=25748612}}</ref>{{Primary source inline|date=November 2020}}

===Protein=== CYP17A1 is a 57.4 kDa protein that belongs to the cytochrome P450 family.<ref>{{cite web |title=CYP17A1 - Steroid 17-alpha-hydroxylase/17,20 lyase - Homo sapiens (Human) - CYP17A1 gene & protein |url=https://www.uniprot.org/uniprot/P05093 |url-status=live |archive-url=https://web.archive.org/web/20161012080551/http://www.uniprot.org/uniprot/P05093 |archive-date=2016-10-12 |access-date=2016-10-11 |website=www.uniprot.org}}</ref><ref>{{cite journal |vauthors=Estrada DF, Laurence JS, Scott EE |date=February 2016 |title=Cytochrome P450 17A1 Interactions with the FMN Domain of Its Reductase as Characterized by NMR |journal=The Journal of Biological Chemistry |volume=291 |issue=8 |pages=3990–4003 |doi=10.1074/jbc.M115.677294 |pmc=4759177 |pmid=26719338 |doi-access=free}}</ref> The protein encoded by its cDNA is composed of 508 amino acid residues. As an enzyme, CYP17A1 possesses an active site that associates with a heme prosthetic group to catalyze biosynthetic reactions.<ref name=":1" /> Based on its known structures while bound to two steroidal inhibitors, abiraterone and galeterone, CYP17A1 possesses the canonical cytochrome P450 fold present in other complex P450 enzymes that participate in steroidogenesis or cholesterol metabolism, though it orients the steroid ligands toward the F and G helices, perpendicular to the heme group, rather than the β1 sheet.<ref>{{cite journal |vauthors=DeVore NM, Scott EE |date=January 2012 |title=Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001 |journal=Nature |volume=482 |issue=7383 |pages=116–119 |bibcode=2012Natur.482..116D |doi=10.1038/nature10743 |pmc=3271139 |pmid=22266943}}</ref><ref>{{cite journal |vauthors=Petrunak EM, DeVore NM, Porubsky PR, Scott EE |date=November 2014 |title=Structures of human steroidogenic cytochrome P450 17A1 with substrates |journal=The Journal of Biological Chemistry |volume=289 |issue=47 |pages=32952–32964 |doi=10.1074/jbc.M114.610998 |pmc=4239641 |pmid=25301938 |doi-access=free}}</ref>

==Expression== Expression of CYP17A1 has been found in all of the traditional steroidogenic tissues except the placenta, including the zona reticularis and zona fasciculata of the adrenal cortex, the Leydig cells of the testes, the thecal cells of the ovaries, and, more recently, in luteinized granulosa cells in ovarian follicles.<ref name="pmid21095220">{{cite journal |vauthors=Storbeck KH, Swart P, Africander D, Conradie R, Louw R, Swart AC |date=April 2011 |title=16α-hydroxyprogesterone: origin, biosynthesis and receptor interaction |journal=Molecular and Cellular Endocrinology |volume=336 |issue=1–2 |pages=92–101 |doi=10.1016/j.mce.2010.11.016 |pmid=21095220 |s2cid=5503049}}</ref> In addition to classical steroidogenic tissue, CYP17A1 has also been detected in the heart, kidney, and adipose tissue.<ref name="pmid21095220" /> In the fetus, CYP17A1 has been reported in the kidney, thymus, and spleen.<ref name="pmid21095220" />

== Function == CYP17A1 is a member of the cytochrome P450 superfamily of enzymes localized in the endoplasmic reticulum. Proteins in this family are monooxygenases that catalyze synthesis of cholesterol, steroids and other lipids and are involved in drug metabolism.<ref name=":0">{{cite web |title=CYP17A1 cytochrome P450 family 17 subfamily A member 1 [Homo sapiens (human)] - Gene - NCBI |url=https://www.ncbi.nlm.nih.gov/gene/1586 |url-status=live |archive-url=https://web.archive.org/web/20150623020708/http://www.ncbi.nlm.nih.gov/gene/1586 |archive-date=2015-06-23 |access-date=2016-09-27 |website=www.ncbi.nlm.nih.gov}}</ref> CYP17A1 has both 17α-hydroxylase activity ({{EC number|1.14.14.19}}) and 17,20-lyase activity ({{EC number|1.14.14.32}}). The 17α-hydroxylase activity of CYP17A1 is required for the generation of glucocorticoids such as cortisol, but both the hydroxylase and 17,20-lyase activities of CYP17A1 are required for the production of androgenic and oestrogenic sex steroids by converting 17α-hydroxypregnenolone to dehydroepiandrosterone (DHEA).<ref>{{cite journal |vauthors=DeVore NM, Scott EE |date=January 2012 |title=Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001 |journal=Nature |volume=482 |issue=7383 |pages=116–119 |bibcode=2012Natur.482..116D |doi=10.1038/nature10743 |pmc=3271139 |pmid=22266943}}</ref> Mutations in this gene are associated with isolated steroid-17α-hydroxylase deficiency, 17α-hydroxylase/17,20-lyase deficiency, pseudohermaphroditism, and adrenal hyperplasia.<ref name=":0"/>

Furthermore, the 17,20-lyase activity is dependent on cytochrome P450 oxidoreductase (POR) cytochrome b5 (CYB5) and phosphorylation.<ref>{{cite journal |vauthors=Udhane SS, Dick B, Hu Q, Hartmann RW, Pandey AV |date=September 2016 |title=Specificity of anti-prostate cancer CYP17A1 inhibitors on androgen biosynthesis |journal=Biochemical and Biophysical Research Communications |volume=477 |issue=4 |pages=1005–1010 |bibcode=2016BBRC..477.1005U |doi=10.1016/j.bbrc.2016.07.019 |pmid=27395338 |doi-access=free}}</ref><ref>{{cite journal |vauthors=Pandey AV, Miller WL |date=April 2005 |title=Regulation of 17,20 lyase activity by cytochrome b5 and by serine phosphorylation of P450c17 |journal=The Journal of Biological Chemistry |volume=280 |issue=14 |pages=13265–13271 |doi=10.1074/jbc.M414673200 |pmid=15687493 |doi-access=free}}</ref><ref name="ReferenceB">{{cite journal |vauthors=Zhang LH, Rodriguez H, Ohno S, Miller WL |date=November 1995 |title=Serine phosphorylation of human P450c17 increases 17,20-lyase activity: implications for adrenarche and the polycystic ovary syndrome |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=92 |issue=23 |pages=10619–10623 |bibcode=1995PNAS...9210619Z |doi=10.1073/pnas.92.23.10619 |pmc=40663 |pmid=7479852 |doi-access=free}}</ref> Cytochrome b5 acts as a facilitator for 17,20 lyase activity of CYP17A1 and can donate a second electron to some P450s. In humans the production of testosterone via pregnenolone to17-OHPreg and DHEA by the CYP17A1 requires POR.<ref>{{cite journal |vauthors=Fukami M, Homma K, Hasegawa T, Ogata T |date=April 2013 |title=Backdoor pathway for dihydrotestosterone biosynthesis: implications for normal and abnormal human sex development |journal=Developmental Dynamics |volume=242 |issue=4 |pages=320–329 |doi=10.1002/dvdy.23892 |pmid=23073980 |s2cid=44702659 |doi-access=free}}</ref><ref name="wj">{{cite journal |vauthors=Masiutin M, Yadav M |year=2023 |title=Alternative androgen pathways |journal=WikiJournal of Medicine |volume=10 |pages=X |doi=10.15347/WJM/2023.003 |s2cid=257943362 |doi-access=free}}</ref> Human CYP17A1 protein is phosphorylated on serine and threonine residues by a cAMP-dependent protein kinase. Phosphorylation of the protein increases 17,20-lyase activity, while dephosphorylation virtually eliminates this activity.<ref name="ReferenceB"/>

==Clinical significance== Mutations in this gene are associated with rare forms of congenital adrenal hyperplasia, specifically 17α-hydroxylase deficiency/17,20-lyase deficiency and isolated 17,20-lyase deficiency.<ref>{{cite web |title=Entrez Gene: CYP17A1 cytochrome P450, family 17, subfamily A, polypeptide 1 |url=https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=1586 |url-status=live |archive-url=https://web.archive.org/web/20100307142011/http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1586 |archive-date=2010-03-07 |access-date=2017-08-30}}</ref>

In humans, the CYP17A1 gene is largely associated with endocrine effects and steroid hormone metabolism.<ref>{{cite journal |vauthors=Ma YN, Cao CY, Wang QW, Gui WJ, Zhu GN |date=October 2016 |title=Effects of azocyclotin on gene transcription and steroid metabolome of hypothalamic-pituitary-gonad axis, and their consequences on reproduction in zebrafish (Danio rerio) |journal=Aquatic Toxicology |volume=179 |pages=55–64 |doi=10.1016/j.aquatox.2016.08.006 |pmid=27571716}}</ref><ref>{{cite journal |vauthors=Legendre A, Elie C, Ramambason C, Manens L, Souidi M, Froment P, Tack K |date=August 2016 |title=Endocrine effects of lifelong exposure to low-dose depleted uranium on testicular functions in adult rat |url=https://hal.science/hal-01407270/file/1-s2.0-S0300483X16301895-main.pdf |url-status=live |journal=Toxicology |volume=368-369 |pages=58–68 |bibcode=2016Toxgy.368...58L |doi=10.1016/j.tox.2016.08.014 |pmid=27544493 |archive-url=https://web.archive.org/web/20240202144956/https://hal.science/hal-01407270/file/1-s2.0-S0300483X16301895-main.pdf |archive-date=2024-02-02 |access-date=2024-02-02 |doi-access=free}}</ref><ref>{{cite journal |vauthors=Yadav R, Petrunak EM, Estrada DF, Scott EE |date=February 2017 |title=Structural insights into the function of steroidogenic cytochrome P450 17A1 |journal=Molecular and Cellular Endocrinology |volume=441 |pages=68–75 |doi=10.1016/j.mce.2016.08.035 |pmc=5235955 |pmid=27566228}}</ref> Furthermore, mutations in the CYP17A1 gene are associated with rare forms of congenital adrenal hyperplasia, in particular 17α-hydroxylase deficiency/17,20-lyase deficiency and isolated 17,20-lyase deficiency. Overall, CYP17A1 is an important target for inhibition in the treatment of prostate cancer because it produces androgen that is required for tumor cell growth.<ref>{{cite journal |vauthors=Kostin VA, Zolottsev VA, Kuzikov AV, Masamrekh RA, Shumyantseva VV, Veselovsky AV, Stulov SV, Novikov RA, Timofeev VP, Misharin AY |date=November 2016 |title=Oxazolinyl derivatives of [17(20)E]-21-norpregnene differing in the structure of A and B rings. Facile synthesis and inhibition of CYP17A1 catalytic activity |journal=Steroids |volume=115 |pages=114–122 |doi=10.1016/j.steroids.2016.06.002 |pmid=27505042 |s2cid=205256638}}</ref><ref name="Bonomo_2016">{{cite journal |vauthors=Bonomo S, Hansen CH, Petrunak EM, Scott EE, Styrishave B, Jørgensen FS, Olsen L |date=July 2016 |title=Promising Tools in Prostate Cancer Research: Selective Non-Steroidal Cytochrome P450 17A1 Inhibitors |journal=Scientific Reports |volume=6 |bibcode=2016NatSR...629468B |doi=10.1038/srep29468 |pmc=4942611 |pmid=27406023 |article-number=29468}}</ref> The decreased enzyme activity of CYP17A1 is related to infertility due to hypogonadotropic hypogonadism. In females, folliculogenesis is arrested, while in males, testicular atrophy with interstitial cell proliferation and arrested spermatogenesis. Although generally anovulatory, there are some case reports of women with 17α-hydroxylase deficiency who underwent spontaneous menarche with cyclic menses.<ref name="pmid33158283">{{cite journal |vauthors=Acién P, Acién M |date=November 2020 |title=Disorders of Sex Development: Classification, Review, and Impact on Fertility |journal=Journal of Clinical Medicine |volume=9 |issue=11 |page=3555 |doi=10.3390/jcm9113555 |pmc=7694247 |pmid=33158283 |doi-access=free}}</ref> {{See also|Congenital adrenal hyperplasia due to 17α-hydroxylase deficiency}}

===Clinical marker=== A multi-locus genetic risk score study based on a combination of 27 loci, including the CYP17A1 gene, identified individuals at increased risk for both incident and recurrent coronary artery disease events, as well as an enhanced clinical benefit from statin therapy. The study was based on a community cohort study (the Malmo Diet and Cancer study) and four additional randomized controlled trials of primary prevention cohorts (JUPITER and ASCOT) and secondary prevention cohorts (CARE and PROVE IT-TIMI 22).<ref name="ReferenceA"/>

==As a drug target== ===CYP17A1 inhibitors=== {{Main|CYP17A1 inhibitor}} In 2011, the FDA approved the CYP17A1 inhibitor, abiraterone, which contains a steroidal scaffold that is similar to the endogenous CYP17A1 substrates, with prednisone for the treatment of castration-resistant prostate cancer. Abiraterone is structurally similar to the substrates of other cytochrome P450 enzymes involved in steroidogenesis, and interference can pose a liability in terms of side effects. Using nonsteroidal scaffolds is expected to enable the design of compounds that interact more selectively with CYP17A1.<ref name = "Bonomo_2016"/> Potent inhibitors of the CYP17A1 enzyme provide a last line defense against ectopic androgenesis in advanced prostate cancer.<ref>{{cite journal |vauthors=Bordeau BM, Ciulla DA, Callahan BP |date=September 2016 |title=Hedgehog Proteins Consume Steroidal CYP17A1 Antagonists: Potential Therapeutic Significance in Advanced Prostate Cancer |journal=ChemMedChem |volume=11 |issue=18 |pages=1983–1986 |doi=10.1002/cmdc.201600238 |pmc=5588864 |pmid=27435344}}</ref>

The drug abiraterone acetate, which is used to treat castration-resistant prostate cancer, blocks the biosynthesis of androgens by inhibiting the CYP17A1 enzyme. Abiraterone acetate binds in the active site of the enzyme<ref>{{cite journal |vauthors=Fernández-Cancio M, Camats N, Flück CE, Zalewski A, Dick B, Frey BM, Monné R, Torán N, Audí L, Pandey AV |date=April 2018 |title=Mechanism of the Dual Activities of Human CYP17A1 and Binding to Anti-Prostate Cancer Drug Abiraterone Revealed by a Novel V366M Mutation Causing 17,20 Lyase Deficiency |journal=Pharmaceuticals |volume=11 |issue=2 |pages=37 |doi=10.3390/ph11020037 |pmc=6027421 |pmid=29710837 |doi-access=free}}</ref> and coordinates the heme iron through its pyridine nitrogen, mimicking the substrate.<ref name="pmid22266943">{{PDB|3ruk}}; {{cite journal |vauthors=DeVore NM, Scott EE |date=January 2012 |title=Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001 |journal=Nature |volume=482 |issue=7383 |pages=116–119 |bibcode=2012Natur.482..116D |doi=10.1038/nature10743 |pmc=3271139 |pmid=22266943}}</ref>

Since 2014, galeterone has been in phase III clinical trials for castration-resistant prostate cancer.<ref name="Tokai2014">{{cite press release |title=Tokai Pharmaceuticals' Reformulated Galeterone Demonstrates Robust PSA Reductions in Advanced Prostate Cancer Patients |date=January 29, 2014 |publisher=Tokai Pharmaceuticals |url=http://investors.tokaipharma.com/phoenix.zhtml?c=252857&p=irol-newsArticle_pf&ID=1953287}}{{Dead link|date=March 2024 |bot=InternetArchiveBot |fix-attempted=yes }}</ref>

Ketoconazole is an older CYP17A1 inhibitor that is now little used. However, ketoconazole competitively inhibits CYP17A1, therefore its effectiveness will depend on the concentration of ketoconazole. This is in contrast to the abiraterone acetate, that permanently (rather than competitively) disables CYP17A1, once it binds to it.{{cn|date=January 2026}}

Seviteronel (VT-464) is a novel CYP17A1 inhibitor which is aimed to avoid co-administration of glucocorticoid therapy.<ref name="pmid27154414">{{cite journal |vauthors=Bird IM, Abbott DH |date=October 2016 |title=The hunt for a selective 17,20 lyase inhibitor; learning lessons from nature |journal=The Journal of Steroid Biochemistry and Molecular Biology |volume=163 |pages=136–146 |doi=10.1016/j.jsbmb.2016.04.021 |pmc=5046225 |pmid=27154414 |quote=VT464 is another recently developed compound proposed to act as a selective lyase inhibitor, and more complete data is available in the public domain to support this claim. A review of preliminary data released suggest the IC50 for Human CYP17 lyase activity is ten times lower than for hydroxylase 15 and in nonhuman primates VT464 was able to suppress circulating testosterone as effectively as abiraterone, but with minimally depressed cortisol (remaining at 82% control compared to only 9% with aberaterone), and without associated increases in pregnenolone, progesterone and mineralocorticoids otherwise observed with abiraterone. Like Galaterone, VT464 is also in use in clinical trials without co-administration of prednisone. Together with the clear lack of suppression of circulating cortisol in nonhuman primates, these data argue that VT464 may indeed be a selective 17,20 lyase inhibitor.}}</ref> In the 2010s, it underwent various phases of clinical studies and preclinical models as a drug against prostate cancer or breast cancer.<ref name="pmid32327394">{{cite journal |vauthors=Madan RA, Schmidt KT, Karzai F, Peer CJ, Cordes LM, Chau CH, Steinberg SM, Owens H, Eisner J, Moore WR, Dahut WL, Gulley JL, Figg WD |date=August 2020 |title=Phase 2 Study of Seviteronel (INO-464) in Patients With Metastatic Castration-Resistant Prostate Cancer After Enzalutamide Treatment |journal=Clinical Genitourinary Cancer |volume=18 |issue=4 |pages=258–267.e1 |doi=10.1016/j.clgc.2019.11.002 |pmc=7415516 |pmid=32327394}}</ref><ref name="pmid31367790">{{cite journal |vauthors=Peer CJ, Schmidt KT, Kindrick JD, Eisner JR, Brown VV, Baskin-Bey E, Madan R, Figg WD |date=October 2019 |title=A population pharmacokinetic analysis of the oral CYP17 lyase and androgen receptor inhibitor seviteronel in patients with advanced/metastatic castration-resistant prostate cancer or breast cancer |journal=Cancer Chemotherapy and Pharmacology |volume=84 |issue=4 |pages=759–770 |doi=10.1007/s00280-019-03908-0 |pmc=8132106 |pmid=31367790 |s2cid=199056344}}</ref>

==Steroidogenesis== {| | [[File:Steroidogenesis.svg|class=skin-invert-image|thumb|none|600px|Steroidogenesis, showing, at left side, both reactions of 17α-hydroxylase, and both actions of 17, 20 lyase.]] |}

==Additional images== <gallery class="skin-invert-image"> File:Pregnenolone.svg|Pregnenolone File:17-Hydroxypregnenolone.svg|17α-Hydroxypregnenolone File:Progesterone.svg|Progesterone File:17-Hydroxyprogesterone.svg|17α-Hydroxyprogesterone File:Trimethyl steroid-nomenclature.svg|Steroid numbering </gallery>

== See also == {{Portal|Biology}} * Steroidogenic enzyme * Cytochrome P450 oxidoreductase deficiency

== References == {{Reflist}}

== Further reading == {{Refbegin|30em}} * {{cite journal |vauthors=Miura K, Yasuda K, Yanase T, Yamakita N, Sasano H, Nawata H, Inoue M, Fukaya T, Shizuta Y |date=October 1996 |title=Mutation of cytochrome P-45017 alpha gene (CYP17) in a Japanese patient previously reported as having glucocorticoid-responsive hyperaldosteronism: with a review of Japanese patients with mutations of CYP17 |journal=The Journal of Clinical Endocrinology and Metabolism |volume=81 |issue=10 |pages=3797–3801 |doi=10.1210/jcem.81.10.8855840 |pmid=8855840 |doi-access=free}} * {{cite journal |vauthors=Miller WL, Geller DH, Auchus RJ |year=1999 |title=The molecular basis of isolated 17,20 lyase deficiency |journal=Endocrine Research |volume=24 |issue=3–4 |pages=817–825 |doi=10.3109/07435809809032692 |pmid=9888582}} * {{cite journal |vauthors=Strauss JF |date=November 2003 |title=Some new thoughts on the pathophysiology and genetics of polycystic ovary syndrome |journal=Annals of the New York Academy of Sciences |volume=997 |issue=1 |pages=42–48 |bibcode=2003NYASA.997...42S |doi=10.1196/annals.1290.005 |pmid=14644808 |s2cid=23559461}} * {{cite journal |vauthors=Haider SM, Patel JS, Poojari CS, Neidle S |date=July 2010 |title=Molecular modeling on inhibitor complexes and active-site dynamics of cytochrome P450 C17, a target for prostate cancer therapy |journal=Journal of Molecular Biology |volume=400 |issue=5 |pages=1078–1098 |doi=10.1016/j.jmb.2010.05.069 |pmid=20595043}} {{Refend}}

== External links == * {{MeshName|CYP17A1+protein,+human}} * {{UCSC gene info|CYP17A1}}

17 Category:Steroid hormone biosynthesis