1a1u: Difference between revisions

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[[Image:1a1u.gif|left|200px]]<br />

[[Image:1a1u.gif|left|200px]]<br /><applet load="1a1u" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1a1u" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1a1u" />

'''SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />

==Overview==

The p53 tumor suppressor oligomerization domain, a dimer of two primary, dimers, is an independently folding domain whose subunits consist of a, beta-strand, a tight turn and an alpha-helix. To evaluate the effect of, hydrophobic side-chains on three-dimensional structure, we substituted, residues Phe341 and Leu344 in the alpha-helix with other hydrophobic amino, acids. Substitutions that resulted in residue 341 having a smaller, side-chain than residue 344 switched the stoichiometry of the domain from, tetrameric to dimeric. The three-dimensional structure of one such dimer, was determined by multidimensional NMR spectroscopy. When compared with, the primary dimer of the wild-type p53 oligomerization domain, the mutant, dimer showed a switch in alpha-helical packing from anti-parallel to, parallel and rotation of the alpha-helices relative to the beta-strands., Hydrophobic side-chain size is therefore an important determinant of a, protein fold.

The p53 tumor suppressor oligomerization domain, a dimer of two primary dimers, is an independently folding domain whose subunits consist of a beta-strand, a tight turn and an alpha-helix. To evaluate the effect of hydrophobic side-chains on three-dimensional structure, we substituted residues Phe341 and Leu344 in the alpha-helix with other hydrophobic amino acids. Substitutions that resulted in residue 341 having a smaller side-chain than residue 344 switched the stoichiometry of the domain from tetrameric to dimeric. The three-dimensional structure of one such dimer was determined by multidimensional NMR spectroscopy. When compared with the primary dimer of the wild-type p53 oligomerization domain, the mutant dimer showed a switch in alpha-helical packing from anti-parallel to parallel and rotation of the alpha-helices relative to the beta-strands. Hydrophobic side-chain size is therefore an important determinant of a protein fold.

==Disease==

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==About this Structure==

1A1U 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1A1U OCA].

1A1U 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=1A1U OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Halezonetis, T.D.]]

[[Category: Halezonetis, T D.]]

[[Category: Mccoy, M.A.]]

[[Category: Mccoy, M A.]]

[[Category: Opella, S.J.]]

[[Category: Opella, S J.]]

[[Category: Stavridi, E.S.]]

[[Category: Stavridi, E S.]]

[[Category: Waterman, J.L.F.]]

[[Category: Waterman, J L.F.]]

[[Category: Wieczorek, A.]]

[[Category: anti-oncogene]]

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[[Category: p53]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 15~~:54:~~25 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:53 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1a1u.gif|left|200px]]<br />
+[[Image:1a1u.gif|left|200px]]<br /><applet load="1a1u" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1a1u" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1a1u" />
 '''SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
 ==Overview==
-The p53 tumor suppressor oligomerization domain, a dimer of two primary, dimers, is an independently folding domain whose subunits consist of a, beta-strand, a tight turn and an alpha-helix. To evaluate the effect of, hydrophobic side-chains on three-dimensional structure, we substituted, residues Phe341 and Leu344 in the alpha-helix with other hydrophobic amino, acids. Substitutions that resulted in residue 341 having a smaller, side-chain than residue 344 switched the stoichiometry of the domain from, tetrameric to dimeric. The three-dimensional structure of one such dimer, was determined by multidimensional NMR spectroscopy. When compared with, the primary dimer of the wild-type p53 oligomerization domain, the mutant, dimer showed a switch in alpha-helical packing from anti-parallel to, parallel and rotation of the alpha-helices relative to the beta-strands., Hydrophobic side-chain size is therefore an important determinant of a, protein fold.
+The p53 tumor suppressor oligomerization domain, a dimer of two primary dimers, is an independently folding domain whose subunits consist of a beta-strand, a tight turn and an alpha-helix. To evaluate the effect of hydrophobic side-chains on three-dimensional structure, we substituted residues Phe341 and Leu344 in the alpha-helix with other hydrophobic amino acids. Substitutions that resulted in residue 341 having a smaller side-chain than residue 344 switched the stoichiometry of the domain from tetrameric to dimeric. The three-dimensional structure of one such dimer was determined by multidimensional NMR spectroscopy. When compared with the primary dimer of the wild-type p53 oligomerization domain, the mutant dimer showed a switch in alpha-helical packing from anti-parallel to parallel and rotation of the alpha-helices relative to the beta-strands. Hydrophobic side-chain size is therefore an important determinant of a protein fold.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-A1U 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A1U OCA].
+A1U 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=1A1U OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Halezonetis, T.D.]]
+[[Category: Halezonetis, T D.]]
-[[Category: Mccoy, M.A.]]
+[[Category: Mccoy, M A.]]
-[[Category: Opella, S.J.]]
+[[Category: Opella, S J.]]
-[[Category: Stavridi, E.S.]]
+[[Category: Stavridi, E S.]]
-[[Category: Waterman, J.L.F.]]
+[[Category: Waterman, J L.F.]]
 [[Category: Wieczorek, A.]]
 [[Category: anti-oncogene]]
@@ Line 29: / Line 28: @@
 [[Category: p53]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:54:25 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:53 2008''