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1a1u

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1a1u, 1 NMR models ()

Gene:

P53 TUMOR SUPPRESSOR (Homo sapiens)

Structural annotation:
Resources:	InterPro : Ipr010991, Ipr015551, Ipr002117, Ipr011615, Ipr013872, Ipr008967, Ipr012346 Pfam : PF07710 SCOP : d1a1ua_, d1a1uc_ UniProt : P04637

Functional annotation:
Cellular component:	cytoplasm nucleolus endoplasmic reticulum insoluble fraction mitochondrion nucleus nucleoplasm nuclear matrix
Biological process:	transcription cellular response to glucose starvation DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis negative regulation of cell cycle nucleotide-excision repair regulation of apoptosis protein complex assembly regulation of mitochondrial membrane permeability protein localization cell cycle arrest negative regulation of helicase activity cell aging base-excision repair multicellular organismal development cell cycle ER overload response apoptosis regulation of transcription, DNA-dependent negative regulation of cell growth cell proliferation response to DNA damage stimulus protein tetramerization cell differentiation induction of apoptosis by intracellular signals caspase activation via cytochrome c
Molecular function:	enzyme binding protein binding DNA strand annealing activity protein heterodimerization activity nuclease activity transcription factor activity zinc ion binding DNA binding protein N-terminus binding ATP binding copper ion binding metal ion binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

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

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1a1u is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

McCoy M, Stavridi ES, Waterman JL, Wieczorek AM, Opella SJ, Halazonetis TD. Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain. EMBO J. 1997 Oct 15;16(20):6230-6. PMID:9321402 doi:10.1093/emboj/16.20.6230
Alibes A, Yankilevich P, Canada A, Diaz-Uriarte R. IDconverter and IDClight: conversion and annotation of gene and protein IDs. BMC Bioinformatics. 2007 Jan 10;8:9. PMID:17214880 doi:10.1186/1471-2105-8-9

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1a1u

From Proteopedia

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

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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