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
Alpha-keratin large variation in α-keratin structures found in mammals. α-keratin synthesis begins near focal adhesions on the cell membrane. There, the keratin filament precursors go through a process known as nucleation, where the keratin precursors of dimers and filaments elongate, fuse, and bundles together. As this synthesis is occurring, the keratin filament precursors are transported by actin fibers in the cell towards the nucleus. There, the alpha-keratin intermediate filaments will collect and form networks of structure dictated by the use of the keratin cell as the nucleus simultaneously degrades. However, if necessary, instead of continuing to grow, the keratin complex will