L-type lectin domain explained
Symbol: | Lectin_leg-like |
Lectin_leg-like |
Pfam: | PF03388 |
Pfam Clan: | CL0004 |
Interpro: | IPR005052 |
Scop: | 1gv9 |
Membranome Family: | 719 |
In molecular biology the L-like lectin domain is a protein domain found in lectins which are similar to the leguminous plant lectins.
Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 and ERGIC-53 lectins.[1] Although proteins containing this domain were originally identified as a family of animal lectins, there are also yeast representatives.[1]
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.[2] Its dysfunction has been associated with combined factors V and VIII deficiency, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein-secreting pathway.[2] [3]
The L-like lectin domain has an overall globular shape composed of a beta-sandwich of two major twisted antiparallel beta-sheets. The beta-sandwich comprises a major concave beta-sheet and a minor convex beta-sheet, in a variation of the jelly roll fold.[4] [5] [6] [7]
Notes and References
- Fiedler K, Simons K . A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins . Cell . 77 . 5 . 625–6 . June 1994 . 8205612 . 10.1016/0092-8674(94)90047-7. 21111364 .
- Itin C, Roche AC, Monsigny M, Hauri HP . ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins . Mol. Biol. Cell . 7 . 3 . 483–93 . March 1996 . 8868475 . 275899 . 10.1091/mbc.7.3.483.
- 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 . ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families . Blood . 93 . 7 . 2261–6 . April 1999 . 10090935 .
- Velloso LM, Svensson K, Schneider G, Pettersson RF, Lindqvist Y . Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum . J. Biol. Chem. . 277 . 18 . 15979–84 . May 2002 . 11850423 . 10.1074/jbc.M112098200 . free .
- Velloso LM, Svensson K, Pettersson RF, Lindqvist Y . 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 . December 2003 . 14643651 . 10.1016/j.jmb.2003.10.031.
- Satoh T, Sato K, Kanoh A, Yamashita K, Yamada Y, Igarashi N, Kato R, Nakano A, Wakatsuki S . Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p . J. Biol. Chem. . 281 . 15 . 10410–9 . April 2006 . 16439369 . 10.1074/jbc.M512258200 . free .
- Satoh T, Cowieson NP, Hakamata W, Ideo H, Fukushima K, Kurihara M, Kato R, Yamashita K, Wakatsuki S . Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36 . J. Biol. Chem. . 282 . 38 . 28246–55 . September 2007 . 17652092 . 10.1074/jbc.M703064200 . 33042130 . free .