1pet: Difference between revisions

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

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

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

caption="1pet" />

'''NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53'''<br />

==Overview==

We report the solution structure of the minimum transforming domain, (residues 303-366) of human p53 (p53tet) determined by multidimensional, NMR spectroscopy. This domain contains a number of important functions, associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase., p53tet forms a symmetric dimer of dimers that is significantly different, from a recent structure reported for a shorter construct of this domain., Phosphorylation of Ser 315 has only minor structural consequences, as this, region of the protein is unstructured. Modelling based on the p53tet, structure suggests possible modes of interaction between adjacent domains, in full-length p53 as well as modes of interaction with DNA.

We report the solution structure of the minimum transforming domain (residues 303-366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA.

==Disease==

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==About this Structure==

1PET 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=1PET OCA].

1PET 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=1PET OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Arrowsmith, C.H.]]

[[Category: Arrowsmith, C H.]]

[[Category: Harvey, T.S.]]

[[Category: Harvey, T S.]]

[[Category: Lee, W.]]

[[Category: Litchfield, D.]]

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[[Category: dna-binding]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:42:~~46 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:04 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1pet.gif|left|200px]]<br />
+[[Image:1pet.gif|left|200px]]<br /><applet load="1pet" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1pet" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1pet" />
 '''NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53'''<br />
 ==Overview==
-We report the solution structure of the minimum transforming domain, (residues 303-366) of human p53 (p53tet) determined by multidimensional, NMR spectroscopy. This domain contains a number of important functions, associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase., p53tet forms a symmetric dimer of dimers that is significantly different, from a recent structure reported for a shorter construct of this domain., Phosphorylation of Ser 315 has only minor structural consequences, as this, region of the protein is unstructured. Modelling based on the p53tet, structure suggests possible modes of interaction between adjacent domains, in full-length p53 as well as modes of interaction with DNA.
+We report the solution structure of the minimum transforming domain (residues 303-366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase. p53tet forms a symmetric dimer of dimers that is significantly different from a recent structure reported for a shorter construct of this domain. Phosphorylation of Ser 315 has only minor structural consequences, as this region of the protein is unstructured. Modelling based on the p53tet structure suggests possible modes of interaction between adjacent domains in full-length p53 as well as modes of interaction with DNA.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-PET 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=1PET OCA].
+PET 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=1PET OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Arrowsmith, C.H.]]
+[[Category: Arrowsmith, C H.]]
-[[Category: Harvey, T.S.]]
+[[Category: Harvey, T S.]]
 [[Category: Lee, W.]]
 [[Category: Litchfield, D.]]
@@ Line 25: / Line 24: @@
 [[Category: dna-binding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:42:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:04 2008''