1hs5
From Proteopedia
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'''NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER''' | '''NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER''' | ||
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[[Category: Ma, W.]] | [[Category: Ma, W.]] | ||
[[Category: Nie, X.]] | [[Category: Nie, X.]] | ||
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| - | [[Category: | + | [[Category: Dimer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:10:48 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:10, 2 May 2008
NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER
Overview
P53 is a homotetrameric tumor suppressor protein involved in transcriptional control of genes that regulate cell proliferation and death. In order to probe the role that oligomerization plays in this capacity, we have previously designed and characterized a series of p53 proteins with altered oligomeric states through hydrophilc substitution of residues Met340 or Leu344 in the normally tetrameric oligomerization domain. Although such mutations have little effect on the overall secondary structural content of the oligomerization domain, both solubility and the resistance to thermal denaturation are substantially reduced relative to that of the wild-type domain. Here, we report the design and characterization of a double-mutant p53 with alterations of residues at positions Met340 and Leu344. The double-mutations Met340Glu/Leu344Lys and Met340Gln/Leu344Arg resulted in distinct dimeric forms of the protein. Furthermore, we have verified by NMR structure determination that the double-mutant Met340Gln/Leu344Arg is essentially a "half-tetramer". Analysis of the in vivo activities of full-length p53 oligomeric mutants reveals that while cell-cycle arrest requires tetrameric p53, transcriptional transactivation activity of monomers and dimers retain roughly background and half of the wild-type activity, respectively.
About this Structure
1HS5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and functionality of a designed p53 dimer., Davison TS, Nie X, Ma W, Lin Y, Kay C, Benchimol S, Arrowsmith CH, J Mol Biol. 2001 Mar 23;307(2):605-17. PMID:11254385 Page seeded by OCA on Fri May 2 19:10:48 2008
