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1olg

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1olg, 1 NMR models ()

Domains:

P53_tetramer

Related:

1olh

Structural annotation:
Resources:	CATH : 1Olga00, 1Olgb00, 1Olgc00, 1Olgd00 InterPro : Ipr011615, Ipr010991, Ipr015551, Ipr013872, Ipr012346, Ipr002117, Ipr008967 Pfam : PF07710 SCOP : d1olga_, d1olgb_, d1olgc_, d1olgd_ UniProt : P04637

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

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR

Publication Abstract from PubMed

The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel beta sheet. One beta strand and one helix are contributed from each monomer. The interface between the two dimers forming the tetramer is mediated solely by helix-helix contacts. The overall result is a symmetric, four-helix bundle with adjacent helices oriented antiparallel to each other and with the two antiparallel beta sheets located on opposing faces of the molecule. The tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. The implications of the structure of the tetramer for the biological function of p53 are discussed.

High-resolution structure of the oligomerization domain of p53 by multidimensional NMR., Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM, Science. 1994 Jul 15;265(5170):386-91. PMID:8023159

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

About this Structure

1OLG is a Single protein structure of sequence from Homo sapiens. Additional information on 1OLG is available in a page on p53 Tumor Suppressor at the RCSB PDB Molecule of the Month. Full experimental information is available from OCA.

Reference

Page seeded by OCA on Wed Jul 23 11:00:24 2008

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1olg

From Proteopedia

HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR

About this Structure

Reference

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