“L-type lectin domain”的意思、由来-开放百科全书

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]

References

1. ^¹{{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| url = }}
2. ^¹{{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| url = }}
3. ^{{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 | doi = | url = }}
4. ^{{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 | url = }}
5. ^{{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| url = }}
6. ^{{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 | url = }}
7. ^{{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 | url = }}