2j11: Difference between revisions

Revision as of 16:50, 27 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:2j11.png

Template:STRUCTURE 2j11

P53 TETRAMERIZATION DOMAIN MUTANT Y327S T329G Q331GP53 TETRAMERIZATION DOMAIN MUTANT Y327S T329G Q331G

Template:ABSTRACT PUBMED 18076077

About this StructureAbout this Structure

2J11 is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach., Mora P, Carbajo RJ, Pineda-Lucena A, Sanchez Del Pino MM, Perez-Paya E, Proteins. 2007 Dec 12;. PMID:18076077

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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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 {{STRUCTURE_2j11|  PDB=2j11  |  SCENE=  }}
-'''P53 TETRAMERIZATION DOMAIN MUTANT Y327S T329G Q331G'''
+===P53 TETRAMERIZATION DOMAIN MUTANT Y327S T329G Q331G===
-==Overview==
+<!--
-The role of hydrophobic amino acids in the formation of hydrophobic cores as one of the major driving forces in protein folding has been extensively studied. However, the implication of neutral solvent-exposed amino acids is less clear and available information is scarce. We have used a combinatorial approach to study the structural relevance of three solvent-exposed residues (Tyr(327), Thr(329), and Gln(331)) located in thebeta-sheet of the tetramerization domain of the tumor suppressor p53 (p53TD). A conformationally defined peptide library was designed where these three positions were randomized. The library was screened for tetramer stability. A set of p53TD mutants containing putative stabilizing or destabilizing residue combinations was synthesized for a thermodynamic characterization. Unfolding experiments showed a wide range of stabilities, with T(m) values between 27 and 83 degrees C. Wild type p53TD and some highly destabilized and stabilized mutants were further characterized. Thermodynamic and biophysical data indicated that these proteins were folded tetramers, with the same overall structure, in equilibrium with unfolded monomers. An NMR study confirmed that the main structural features of p53TD are conserved in all the mutants analyzed. The thermodynamic stability of the different p53TD mutants showed a strong correlation with parameters that favor formation and stabilization of the beta-sheet. We propose that stabilization through hydrophobic interactions of key secondary structure elements might be the underlying mechanism for the strong influence of solvent-exposed residues in the stability of p53TD. Proteins 2007. (c) 2007 Wiley-Liss, Inc.
+The line below this paragraph, {{ABSTRACT_PUBMED_18076077}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18076077 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18076077}}
 ==About this Structure==
-J11 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J11 OCA].
+J11 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J11 OCA].
 ==Reference==
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 [[Category: Transcription regulation]]
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