L-type lectin domain
From Wikipedia, the free encyclopedia
| 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 | ||||||||
| |||||||||
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]