1pet: Difference between revisions

Revision as of 03:33, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pet.png

Template:STRUCTURE 1pet

NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53

Template:ABSTRACT PUBMED 7773777

About this StructureAbout this Structure

1PET is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Solution structure of the tetrameric minimum transforming domain of p53., Lee W, Harvey TS, Yin Y, Yau P, Litchfield D, Arrowsmith CH, Nat Struct Biol. 1994 Dec;1(12):877-90. PMID:7773777

Page seeded by OCA on Mon Jul 28 03:33:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1pet.gif|left|200px]]
+{{Seed}}
+[[Image:1pet.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1pet|  PDB=1pet  |  SCENE=  }}
-'''NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53'''
+===NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7773777}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7773777 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7773777}}
 ==About this Structure==
-PET is a [[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].
+PET is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PET OCA].
 ==Reference==
@@ Line 29: / Line 33: @@
 [[Category: Yin, Y.]]
 [[Category: Dna-binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:00:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:33:00 2008''