L-type lectin domain

In molecular biology the L-like lectin domain is a protein domain found in lectins which are similar to the leguminous plant lectins.

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: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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]