EVH1 Domain
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EVH1 Domain
WH1 domains, also known as EVH1 domains, are evolutionary conserved protein domain, protein domains found on WASP (VASP) proteins, which are often involved in actin polymerization. Function WH1 domains are important for all cellular processes involving actin, this includes cell motility, cell trafficking, cell division and cytokinesis, cell signalling, and the establishment and maintenance of cell junctions and cell shape. Structure Protein tertiary structure, Tertiary structure of the WH1 domain of the ENAH (gene), Mena protein revealed cis-regulatory element, structure similarities with the pleckstrin homology domain, pleckstrin (PH) domain. The overall protein folding, fold consists of a compact parallel beta-sandwich, closed along one edge by a long alpha helix. A highly conservation (genetics), conserved cluster of three surface-exposed aromatic Side chain, side-chains forms the recognition site for the molecule's target ligand (biochemistry), ligands. Interactions The WAS ...
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Protein Domain
In molecular biology, a protein domain is a region of a protein's Peptide, polypeptide chain that is self-stabilizing and that Protein folding, folds independently from the rest. Each domain forms a compact folded Protein tertiary structure, three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or Disulfide bond, disulfide bridges. Domains often form functional units, such as the calcium-binding EF-hand, EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimera (protein), chimeric ...
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