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'''HUMAN VASP TETRAMERISATION DOMAIN''' | '''HUMAN VASP TETRAMERISATION DOMAIN''' | ||
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[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
[[Category: Wolf, E.]] | [[Category: Wolf, E.]] | ||
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Revision as of 08:37, 3 May 2008
HUMAN VASP TETRAMERISATION DOMAIN
Overview
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.
About this Structure
1USE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 11:37:34 2008
