1usd: Difference between revisions
New page: left|200px<br /> <applet load="1usd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1usd, resolution 1.7Å" /> '''HUMAN VASP TETRAMERI... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1usd.gif|left|200px]]<br /> | [[Image:1usd.gif|left|200px]]<br /><applet load="1usd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1usd" size=" | |||
caption="1usd, resolution 1.7Å" /> | caption="1usd, resolution 1.7Å" /> | ||
'''HUMAN VASP TETRAMERISATION DOMAIN L352M'''<br /> | '''HUMAN VASP TETRAMERISATION DOMAIN L352M'''<br /> | ||
==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== | ||
1USD 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:// | 1USD 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=1USD OCA]. | ||
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[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.]] | ||
| Line 25: | Line 24: | ||
[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:43 2008'' | ||
Revision as of 13:27, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 15:27:43 2008
