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1use
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of | + | 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== | ==About this Structure== | ||
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[[Category: Kuhnel, K.]] | [[Category: Kuhnel, K.]] | ||
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
| - | [[Category: Strelkov, S | + | [[Category: Strelkov, S V.]] |
[[Category: Walter, U.]] | [[Category: Walter, U.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
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[[Category: null]] | [[Category: null]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:46 2008'' |
Revision as of 13:27, 21 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
Page seeded by OCA on Thu Feb 21 15:27:46 2008
