1olh: Difference between revisions

Revision as of 14:43, 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:1olh.png

Template:STRUCTURE 1olh

HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMRHIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR

Template:ABSTRACT PUBMED 8023159

About this StructureAbout this Structure

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

ReferenceReference

High-resolution structure of the oligomerization domain of p53 by multidimensional NMR., Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM, Science. 1994 Jul 15;265(5170):386-91. PMID:8023159

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

OCA

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-[[Image:1olh.gif|left|200px]]
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 {{STRUCTURE_1olh|  PDB=1olh  |  SCENE=  }}
-'''HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR'''
+===HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR===
-==Overview==
+<!--
-The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel beta sheet. One beta strand and one helix are contributed from each monomer. The interface between the two dimers forming the tetramer is mediated solely by helix-helix contacts. The overall result is a symmetric, four-helix bundle with adjacent helices oriented antiparallel to each other and with the two antiparallel beta sheets located on opposing faces of the molecule. The tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. The implications of the structure of the tetramer for the biological function of p53 are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_8023159}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8023159 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8023159}}
 ==About this Structure==
-OLH 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=1OLH OCA].
+OLH 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=1OLH OCA].
 ==Reference==
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 [[Category: Omichinski, J G.]]
 [[Category: Anti-oncogene protein]]
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