1olg: Difference between revisions

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[[Image:1olg.gif|left|200px]]
[[Image:1olg.png|left|200px]]


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==Overview==
{{ABSTRACT_8023159}}
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.


==About this Structure==
==About this Structure==
1OLG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1OLG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb31_1.html p53 Tumor Suppressor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLG OCA].  
1OLG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1OLG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb31_1.html p53 Tumor Suppressor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLG OCA].  
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/8023159 8023159]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Omichinski, J G.]]
[[Category: Omichinski, J G.]]
[[Category: Anti-oncogene]]
[[Category: Anti-oncogene]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:59:54 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:47:46 2008''

Revision as of 14:47, 26 June 2008

File:1olg.png

Template:STRUCTURE 1olg

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


Template:ABSTRACT 8023159

About this Structure

1OLG is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1OLG with [p53 Tumor Suppressor]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 17:47:46 2008

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