1use: Difference between revisions
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'''HUMAN VASP TETRAMERISATION DOMAIN'''<br /> | '''HUMAN VASP TETRAMERISATION DOMAIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1USE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1USE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: null]] | [[Category: null]] | ||
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Revision as of 15:03, 15 February 2008
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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
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