2j10

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(New page: 200px<br /> <applet load="2j10" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j10" /> '''P53 TETRAMERIZATION DOMAIN MUTANT T329F Q33...)
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[[Image:2j10.gif|left|200px]]<br />
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[[Image:2j10.jpg|left|200px]]<br /><applet load="2j10" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2j10" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2j10" />
caption="2j10" />
'''P53 TETRAMERIZATION DOMAIN MUTANT T329F Q331K'''<br />
'''P53 TETRAMERIZATION DOMAIN MUTANT T329F Q331K'''<br />
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==Disease==
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==Overview==
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Known diseases associated with this structure: Adrenal cortical carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Breast cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Colorectal cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Hepatocellular carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Histiocytoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Li-Fraumeni syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Multiple malignancy syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Nasopharyngeal carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Osteosarcoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Pancreatic cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Thyroid carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]]
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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.
==About this Structure==
==About this Structure==
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2J10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J10 OCA].
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2J10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J10 OCA].
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==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18076077 18076077]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Carbajo, R.J.]]
[[Category: Carbajo, R.J.]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:50:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:22:25 2008''

Revision as of 09:22, 23 January 2008

Image:2j10.jpg

2j10

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P53 TETRAMERIZATION DOMAIN MUTANT T329F Q331K

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.

About this Structure

2J10 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

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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