1A1U

SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1A1U

• Entry DOI: 10.2210/pdb1a1u/pdb
• Descriptor: P53 (1 entity in total)
• Functional Keywords: p53, oligomerization domain, human, anti-oncogene
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
• Total number of polymer chains: 2
• Total formula weight: 8421.28

Authors

Mccoy, M.A.,Stavridi, E.S.,Waterman, J.L.F.,Wieczorek, A.,Opella, S.J.,Halezonetis, T.D. (deposition date: 1997-12-16, release date: 1998-04-08, Last modification date: 2024-05-22)

Primary citation

McCoy, M.,Stavridi, E.S.,Waterman, J.L.,Wieczorek, A.M.,Opella, S.J.,Halazonetis, T.D.
Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain.
EMBO J., 16:6230-6236, 1997

PubMed Abstract: 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.

PubMed: 9321402
DOI: 10.1093/emboj/16.20.6230

Experimental method

SOLUTION NMR