1use

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[[Image:1use.jpg|left|200px]]<br /><applet load="1use" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1use.jpg|left|200px]]
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caption="1use, resolution 1.3&Aring;" />
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'''HUMAN VASP TETRAMERISATION DOMAIN'''<br />
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{{Structure
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|PDB= 1use |SIZE=350|CAPTION= <scene name='initialview01'>1use</scene>, resolution 1.3&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''HUMAN VASP TETRAMERISATION DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15569942 15569942]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:46 2008''
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''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

Image:1use.jpg


PDB ID 1use

Drag the structure with the mouse to rotate
, resolution 1.3Å
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

Page seeded by OCA on Thu Mar 20 14:36:04 2008

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