1use: Difference between revisions

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==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.

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==

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[[Category: Kuhnel, K.]]

[[Category: Schlichting, I.]]

[[Category: Strelkov, S.V.]]

[[Category: Strelkov, S V.]]

[[Category: Walter, U.]]

[[Category: Wittinghofer, A.]]

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[[Category: null]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 16: / Line 16: @@
 [[Category: Kuhnel, K.]]
 [[Category: Schlichting, I.]]
-[[Category: Strelkov, S.V.]]
+[[Category: Strelkov, S V.]]
 [[Category: Walter, U.]]
 [[Category: Wittinghofer, A.]]
@@ Line 22: / Line 22: @@
 [[Category: null]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:03:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:46 2008''