1use: Difference between revisions
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'''HUMAN VASP TETRAMERISATION DOMAIN''' | {{Structure | ||
|PDB= 1use |SIZE=350|CAPTION= <scene name='initialview01'>1use</scene>, resolution 1.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''HUMAN VASP TETRAMERISATION DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1USE is a [ | 1USE is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15569942 15569942] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: null]] | [[Category: null]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:36:04 2008'' | ||
Revision as of 12:36, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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