# L-type lectin domain

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Protein family

Lectin_leg-like 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 Identifiers Symbol Lectin_leg-like Pfam PF03388 Pfam clan CL0004 InterPro IPR005052 SCOP2 1gv9 / SCOPe / SUPFAM Membranome 719 Available protein structures: PDB IPR005052 PF03388 (ECOD; PDBsum) AlphaFold IPR005052 PF03388

In molecular biology the **L-like lectin domain** is a [protein domain](/source/Protein_domain) found in [lectins](/source/Lectins) which are similar to the [leguminous plant lectins](/source/Leguminous_lectin_family).

Lectins are structurally diverse [proteins](/source/Protein) that [bind](/source/Molecular_binding) to specific [carbohydrates](/source/Carbohydrate). This family includes the [VIP36](/source/LMAN2L) and [ERGIC-53](/source/ERGIC-53) [lectins](/source/Lectin).[1] Although proteins containing this domain were originally identified as a family of animal lectins, there are also [yeast](/source/Saccharomyces_cerevisiae) representatives.[1]

ERGIC-53 is a 53kDa protein, localised to the intermediate region between the [endoplasmic reticulum](/source/Endoplasmic_reticulum) and the [Golgi apparatus](/source/Golgi_apparatus) (ER-Golgi-Intermediate Compartment, ERGIC). It was identified as a [calcium](/source/Calcium)-dependent, [mannose](/source/Mannose)-specific lectin.[2] Its [dysfunction](https://en.wiktionary.org/wiki/dysfunction) has been associated with combined [factors V](/source/Factor_V_deficiency) and [VIII](/source/Factor_VIII_deficiency) deficiency, suggesting an important and substrate-specific role for ERGIC-53 in the [glycoprotein](/source/Glycoprotein)-secreting pathway.[2][3]

The L-like lectin domain has an overall globular shape composed of a [beta-sandwich](/source/Beta-sandwich) of two major twisted [antiparallel](/source/Antiparallel_(biochemistry)) [beta-sheets](/source/Beta-sheet). The beta-sandwich comprises a major [concave](https://en.wiktionary.org/wiki/concave) beta-sheet and a minor [convex](https://en.wiktionary.org/wiki/convex) beta-sheet, in a variation of the [jelly roll fold](/source/Jelly_roll_fold).[4][5][6][7]

## References

1. ^ [***a***](#cite_ref-pmid8205612_1-0) [***b***](#cite_ref-pmid8205612_1-1) Fiedler K, Simons K (June 1994). "A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins". *Cell*. **77** (5): 625–6. [doi](/source/Doi_(identifier)):[10.1016/0092-8674(94)90047-7](https://doi.org/10.1016%2F0092-8674%2894%2990047-7). [PMID](/source/PMID_(identifier)) [8205612](https://pubmed.ncbi.nlm.nih.gov/8205612). [S2CID](/source/S2CID_(identifier)) [21111364](https://api.semanticscholar.org/CorpusID:21111364).

1. ^ [***a***](#cite_ref-pmid8868475_2-0) [***b***](#cite_ref-pmid8868475_2-1) Itin C, Roche AC, Monsigny M, Hauri HP (March 1996). ["ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC275899). *Mol. Biol. Cell*. **7** (3): 483–93. [doi](/source/Doi_(identifier)):[10.1091/mbc.7.3.483](https://doi.org/10.1091%2Fmbc.7.3.483). [PMC](/source/PMC_(identifier)) [275899](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC275899). [PMID](/source/PMID_(identifier)) [8868475](https://pubmed.ncbi.nlm.nih.gov/8868475).

1. **[^](#cite_ref-pmid10090935_3-0)** 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 (April 1999). "ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families". *Blood*. **93** (7): 2261–6. [PMID](/source/PMID_(identifier)) [10090935](https://pubmed.ncbi.nlm.nih.gov/10090935).

1. **[^](#cite_ref-pmid11850423_4-0)** Velloso LM, Svensson K, Schneider G, Pettersson RF, Lindqvist Y (May 2002). ["Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum"](https://doi.org/10.1074%2Fjbc.M112098200). *J. Biol. Chem*. **277** (18): 15979–84. [doi](/source/Doi_(identifier)):[10.1074/jbc.M112098200](https://doi.org/10.1074%2Fjbc.M112098200). [PMID](/source/PMID_(identifier)) [11850423](https://pubmed.ncbi.nlm.nih.gov/11850423).

1. **[^](#cite_ref-pmid14643651_5-0)** Velloso LM, Svensson K, Pettersson RF, Lindqvist Y (December 2003). "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". *J. Mol. Biol*. **334** (5): 845–51. [doi](/source/Doi_(identifier)):[10.1016/j.jmb.2003.10.031](https://doi.org/10.1016%2Fj.jmb.2003.10.031). [PMID](/source/PMID_(identifier)) [14643651](https://pubmed.ncbi.nlm.nih.gov/14643651).

1. **[^](#cite_ref-pmid16439369_6-0)** Satoh T, Sato K, Kanoh A, Yamashita K, Yamada Y, Igarashi N, Kato R, Nakano A, Wakatsuki S (April 2006). ["Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p"](https://doi.org/10.1074%2Fjbc.M512258200). *J. Biol. Chem*. **281** (15): 10410–9. [doi](/source/Doi_(identifier)):[10.1074/jbc.M512258200](https://doi.org/10.1074%2Fjbc.M512258200). [PMID](/source/PMID_(identifier)) [16439369](https://pubmed.ncbi.nlm.nih.gov/16439369).

1. **[^](#cite_ref-pmid17652092_7-0)** Satoh T, Cowieson NP, Hakamata W, Ideo H, Fukushima K, Kurihara M, Kato R, Yamashita K, Wakatsuki S (September 2007). ["Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36"](http://espace.library.uq.edu.au/view/UQ:130028/UQ130028_OA.pdf) (PDF). *J. Biol. Chem*. **282** (38): 28246–55. [doi](/source/Doi_(identifier)):[10.1074/jbc.M703064200](https://doi.org/10.1074%2Fjbc.M703064200). [PMID](/source/PMID_(identifier)) [17652092](https://pubmed.ncbi.nlm.nih.gov/17652092). [S2CID](/source/S2CID_(identifier)) [33042130](https://api.semanticscholar.org/CorpusID:33042130).

This article incorporates text from the public domain [Pfam](/source/Pfam) and [InterPro](/source/InterPro): [IPR005052](https://www.ebi.ac.uk/interpro/entry/IPR005052)

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Adapted from the Wikipedia article [L-type lectin domain](https://en.wikipedia.org/wiki/L-type_lectin_domain) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/L-type_lectin_domain?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.