1usd
From Proteopedia
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| - | [[Image:1usd.gif|left|200px]] | + | [[Image:1usd.gif|left|200px]] |
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| - | '''HUMAN VASP TETRAMERISATION DOMAIN L352M''' | + | {{Structure |
| + | |PDB= 1usd |SIZE=350|CAPTION= <scene name='initialview01'>1usd</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN VASP TETRAMERISATION DOMAIN L352M''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1USD is a [ | + | 1USD 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=1USD 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: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''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 14:36:03 2008'' |
Revision as of 12:36, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN VASP TETRAMERISATION DOMAIN L352M
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
1USD 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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