{{Infobox protein family | Symbol = Lectin_leg-like | Name = Lectin_leg-like | image = PDB 1r1z EBI.jpg | width = | caption = the crystal structure of the carbohydrate recognition domain of the glycoprotein sorting receptor p58/ergic-53 reveals a novel metal binding site and conformational changes associated with calcium ion binding | Pfam = PF03388 | Pfam_clan = CL0004 | InterPro = IPR005052 | SMART = | PROSITE = | MEROPS = | SCOP = 1gv9 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = | Membranome family = 719 }} In molecular biology the '''L-like lectin domain''' is a [[protein domain]] found in [[lectins]] which are similar to the [[leguminous lectin family|leguminous plant lectins]].

Lectins are structurally diverse [[protein]]s that [[Molecular binding|bind]] to specific [[carbohydrate]]s. This family includes the [[LMAN2L|VIP36]] and [[ERGIC-53]] [[lectin]]s.<ref name="pmid8205612">{{cite journal |vauthors=Fiedler K, Simons K | title = A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins | journal = Cell | volume = 77 | issue = 5 | pages = 625–6 |date=June 1994 | pmid = 8205612 | doi = 10.1016/0092-8674(94)90047-7| s2cid = 21111364 }}</ref> Although proteins containing this domain were originally identified as a family of animal lectins, there are also [[Saccharomyces cerevisiae|yeast]] representatives.<ref name="pmid8205612"/>

ERGIC-53 is a 53kDa protein, localised to the intermediate region between the [[endoplasmic reticulum]] and the [[Golgi apparatus]] (ER-Golgi-Intermediate Compartment, ERGIC). It was identified as a [[calcium]]-dependent, [[mannose]]-specific lectin.<ref name="pmid8868475">{{cite journal |vauthors=Itin C, Roche AC, Monsigny M, Hauri HP | title = ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins | journal = Mol. Biol. Cell | volume = 7 | issue = 3 | pages = 483–93 |date=March 1996 | pmid = 8868475 | pmc = 275899 | doi = 10.1091/mbc.7.3.483}}</ref> Its [[wikt:dysfunction|dysfunction]] has been associated with combined [[Factor V deficiency|factors V]] and [[Factor VIII deficiency|VIII]] deficiency, suggesting an important and substrate-specific role for ERGIC-53 in the [[glycoprotein]]-secreting pathway.<ref name="pmid8868475"/><ref name="pmid10090935">{{cite journal |vauthors=Nichols WC, Terry VH, Wheatley MA, Yang A, Zivelin A, Ciavarella N, Stefanile C, Matsushita T, Saito H, de Bosch NB, Ruiz-Saez A, Torres A, Thompson AR, Feinstein DI, White GC, Negrier C, Vinciguerra C, Aktan M, Kaufman RJ, Ginsburg D, Seligsohn U | title = ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families | journal = Blood | volume = 93 | issue = 7 | pages = 2261–6 |date=April 1999 | pmid = 10090935 }}</ref>

The L-like lectin domain has an overall globular shape composed of a [[beta-sandwich]] of two major twisted [[antiparallel (biochemistry)|antiparallel]] [[beta-sheet]]s. The beta-sandwich comprises a major [[wikt:concave|concave]] beta-sheet and a minor [[wikt:convex|convex]] beta-sheet, in a variation of the [[jelly roll fold]].<ref name="pmid11850423">{{cite journal |vauthors=Velloso LM, Svensson K, Schneider G, Pettersson RF, Lindqvist Y | title = Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum | journal = J. Biol. Chem. | volume = 277 | issue = 18 | pages = 15979–84 |date=May 2002 | pmid = 11850423 | doi = 10.1074/jbc.M112098200 | doi-access = free }}</ref><ref name="pmid14643651">{{cite journal |vauthors=Velloso LM, Svensson K, Pettersson RF, Lindqvist Y | title = The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding | journal = J. Mol. Biol. | volume = 334 | issue = 5 | pages = 845–51 |date=December 2003 | pmid = 14643651 | doi = 10.1016/j.jmb.2003.10.031}}</ref><ref name="pmid16439369">{{cite journal |vauthors=Satoh T, Sato K, Kanoh A, Yamashita K, Yamada Y, Igarashi N, Kato R, Nakano A, Wakatsuki S | title = Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p | journal = J. Biol. Chem. | volume = 281 | issue = 15 | pages = 10410–9 |date=April 2006 | pmid = 16439369 | doi = 10.1074/jbc.M512258200 | doi-access = free }}</ref><ref name="pmid17652092">{{cite journal |vauthors=Satoh T, Cowieson NP, Hakamata W, Ideo H, Fukushima K, Kurihara M, Kato R, Yamashita K, Wakatsuki S | title = Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36 | journal = J. Biol. Chem. | volume = 282 | issue = 38 | pages = 28246–55 |date=September 2007 | pmid = 17652092 | doi = 10.1074/jbc.M703064200 | s2cid = 33042130 | url =http://espace.library.uq.edu.au/view/UQ:130028/UQ130028_OA.pdf | doi-access = free }}</ref>

==References== {{reflist}} {{InterPro content|IPR005052}}

[[Category:Protein families]]