L-type lectin domain 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 this domain were originally identified as a family of animal lectins, there are also yeast representatives. 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. Its dysfunction has been associated with combined factors V
Myosin cells, the long coiled-coil tails of the individual myosin molecules join together, forming the thick filaments of the sarcomere. The force-producing head domains stick out from the side of the thick filament, ready to walk along the adjacent actin-based thin filaments in response to the proper chemical signals. Myosin III is a poorly understood member of the myosin family. It has been studied "in vivo" in the eyes of "Drosophila", where it is thought to play a role in phototransduction. A human homologue gene for myosin III, MYO3A, has been uncovered through the Human Genome Project and is expressed in