1use | pdb_00001use

HUMAN VASP TETRAMERISATION DOMAIN

spinqualitylabelsall models 1use, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1use is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1egx, 1jng, 1usd Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-A resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed alpha-helical coiled-coil structure with a similar degree of supercoiling as found in the widespread left-handed coiled coils with heptad repeats. The basis for the right-handed geometry of VASP TD is a 15-residue repeat in its amino acid sequence, which reveals a characteristic pattern of hydrophobic residues. Hydrophobic interactions and a network of salt bridges render VASP TD highly thermostable with a melting point of 120 degrees C. The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.,Kuhnel K, Jarchau T, Wolf E, Schlichting I, Walter U, Wittinghofer A, Strelkov SV Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17027-32. Epub 2004 Nov 29. PMID:15569942 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also MUZIC:Mena VASP Vasodilator-stimulated phosphoprotein

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