L-type lectin domain and VIII deficiency, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein-secreting pathway. 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. 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. Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 and ERGIC-53 lectins. Although proteins containging
Collagen receptor N-terminal domain rich in cystein, F2 fibronectin type II domain and several C-lectin domains. From this mannose family, collagen is specifically bound by mannose receptor, M-phospholipase A2 receptor and Endo180 receptor. Binding of collagen or denatured collagen (gelatin) is provided by F2 domain and partly by C-terminal domain (aa 1000-1453), which binds type I collagen triple helix. Inability to internalize collagen and reduced ability of adhesion and related increased migration in collagen matrix was observed in fibroblast population with nonfunctional Endo180 receptor. The exact principal of collagen binding to mannose receptor is not known so far. Endo180 receptor is expressed