2j10
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2j10.jpg|left|200px]] | [[Image:2j10.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2j10", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2j10| PDB=2j10 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''P53 TETRAMERIZATION DOMAIN MUTANT T329F Q331K''' | '''P53 TETRAMERIZATION DOMAIN MUTANT T329F Q331K''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2J10 is a [[Single protein]] structure | + | 2J10 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J10 OCA]. |
==Reference== | ==Reference== | ||
| Line 29: | Line 26: | ||
[[Category: Pineda-Lucena, A.]] | [[Category: Pineda-Lucena, A.]] | ||
[[Category: Pino, M M.Sanchez Del.]] | [[Category: Pino, M M.Sanchez Del.]] | ||
| - | [[Category: | + | [[Category: Acetylation]] |
| - | [[Category: | + | [[Category: Activator]] |
| - | [[Category: | + | [[Category: Alternative splicing]] |
| - | [[Category: | + | [[Category: Anti-oncogene]] |
| - | [[Category: | + | [[Category: Apoptosis]] |
| - | [[Category: | + | [[Category: Cell cycle]] |
| - | [[Category: | + | [[Category: Disease mutation]] |
| - | [[Category: | + | [[Category: Dna-binding]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Host-virus interaction]] |
| - | [[Category: | + | [[Category: Li-fraumeni syndrome]] |
| - | [[Category: | + | [[Category: Metal-binding]] |
| - | [[Category: | + | [[Category: Nuclear protein]] |
| - | [[Category: | + | [[Category: P53]] |
| - | [[Category: | + | [[Category: Phosphorylation]] |
| - | [[Category: | + | [[Category: Polymorphism]] |
| - | [[Category: | + | [[Category: Tetramerization domain]] |
| - | [[Category: | + | [[Category: Transcription]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | [[Category: | + | [[Category: Wild type]] |
| - | [[Category: | + | [[Category: Zinc]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:11:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:11, 4 May 2008
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. 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 Page seeded by OCA on Sun May 4 08:11:41 2008
Categories: Single protein | Carbajo, R J. | Mora, P. | Perez-Paya, E. | Pineda-Lucena, A. | Pino, M M.Sanchez Del. | Acetylation | Activator | Alternative splicing | Anti-oncogene | Apoptosis | Cell cycle | Disease mutation | Dna-binding | Glycoprotein | Host-virus interaction | Li-fraumeni syndrome | Metal-binding | Nuclear protein | P53 | Phosphorylation | Polymorphism | Tetramerization domain | Transcription | Transcription regulation | Wild type | Zinc
