1usd: Difference between revisions

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[[Image:1usd.gif|left|200px]]
{{Seed}}
[[Image:1usd.png|left|200px]]


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{{STRUCTURE_1usd|  PDB=1usd  |  SCENE=  }}  
{{STRUCTURE_1usd|  PDB=1usd  |  SCENE=  }}  


'''HUMAN VASP TETRAMERISATION DOMAIN L352M'''
===HUMAN VASP TETRAMERISATION DOMAIN L352M===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_15569942}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15569942}}


==About this Structure==
==About this Structure==
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[[Category: Kinase]]
[[Category: Kinase]]
[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
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