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1use

From Proteopedia

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{{STRUCTURE_1use| PDB=1use | SCENE= }}
{{STRUCTURE_1use| PDB=1use | SCENE= }}
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'''HUMAN VASP TETRAMERISATION DOMAIN'''
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===HUMAN VASP TETRAMERISATION DOMAIN===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15569942}}
==About this Structure==
==About this Structure==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:35:29 2008''

Revision as of 04:35, 28 July 2008

Image:1use.png

Template:STRUCTURE 1use

HUMAN VASP TETRAMERISATION DOMAIN

Template:ABSTRACT PUBMED 15569942

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 Mon Jul 28 07:35:29 2008

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