1a1u
From Proteopedia
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'''SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE''' | '''SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE''' | ||
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[[Category: Waterman, J L.F.]] | [[Category: Waterman, J L.F.]] | ||
[[Category: Wieczorek, A.]] | [[Category: Wieczorek, A.]] | ||
| - | [[Category: | + | [[Category: Anti-oncogene]] |
| - | [[Category: | + | [[Category: Human]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[Category: Oligomerization domain]] |
| - | [[Category: | + | [[Category: P53]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:40:55 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:40, 2 May 2008
SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
The p53 tumor suppressor oligomerization domain, a dimer of two primary dimers, is an independently folding domain whose subunits consist of a beta-strand, a tight turn and an alpha-helix. To evaluate the effect of hydrophobic side-chains on three-dimensional structure, we substituted residues Phe341 and Leu344 in the alpha-helix with other hydrophobic amino acids. Substitutions that resulted in residue 341 having a smaller side-chain than residue 344 switched the stoichiometry of the domain from tetrameric to dimeric. The three-dimensional structure of one such dimer was determined by multidimensional NMR spectroscopy. When compared with the primary dimer of the wild-type p53 oligomerization domain, the mutant dimer showed a switch in alpha-helical packing from anti-parallel to parallel and rotation of the alpha-helices relative to the beta-strands. Hydrophobic side-chain size is therefore an important determinant of a protein fold.
About this Structure
1A1U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain., McCoy M, Stavridi ES, Waterman JL, Wieczorek AM, Opella SJ, Halazonetis TD, EMBO J. 1997 Oct 15;16(20):6230-6. PMID:9321402 Page seeded by OCA on Fri May 2 09:40:55 2008
