Von Willebrand factor type D domain Von Willebrand factor type D domain is an evolutionarilly-conserved protein domain found in, among others, the von Willebrand factor . vWF is a large multimeric glycoprotein and it is synthesized by a type of bone marrow cell called megakaryocytes . The vWD domain allows vWF to perform its blood-clotting function by carrying factor VIII around.Structure The D8 domain is a highly structured region containing 24 paired cysteine residues. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands in the larger vWF protein . vWD is visible as lobes in cryo-EM images of the vWF. In a "D" domain of the vWF it is associated with a few other cysteine-rich domains named C8 , TIL and vWE. A crystal structure for the "D" domains in vWF was solved in 2018. The VWD domain proper and the vWE domain are composed mostly of antiparallel beta sheets . C8 folds into a few helices. TIL is mostly loops with a triad of beta sheets. VWD also contains a calcium binding site . All these domains are disulfide rich.Function The vWD domain D'/D3 of the von Willebrand factor serves as a carrier of clotting factor VIII. The native conformation of the D' domain of vWF is not only required for factor VIII binding but also for normal multimerisation and optimal secretion . The interaction between blood clotting factor VIII and VWF is necessary for normal survival of blood clotting factor VIII in blood circulation . The VWFD domain is a highly structured region, in which the first conserved Cys has been found to form a disulphide bridge with the second conserved one. The other D domains in the protein are necessary for multimerisation. This domain is found in mucins, in zonadhesin , in otogelin , and in vitellogenin . Many of these proteins are extracellular glycoproteins. It is also found in a Cypridina-luciferin 2-monooxygenase . Its actual functions in these proteins are unknown.
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