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1aie

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1aie, resolution 1.50Å ()

Structural annotation:
Resources:	InterPro : Ipr015551, Ipr013872, Ipr010991, Ipr012346, Ipr011615, Ipr008967, Ipr002117 Pfam : PF07710 SCOP : d1aie__ UniProt : P04637

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

P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE

Publication Abstract from PubMed

The molecular replacement method is a powerful technique for crystal structure solution but the use of NMR structures as templates often causes problems. In this work the NMR structure of the p53 tetramerization domain has been used to solve the crystal structure by molecular replacement. Since the rotation- and translation-functions were not sufficiently clear, additional information about the symmetry of the crystal and the protein complex was used to identify correct solutions. The three-dimensional structure of residues 326-356 was subsequently refined to a final R factor of 19.1% at 1.5 A resolution.

Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template., Mittl PR, Chene P, Grutter MG, Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):86-9. PMID:9761820

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

About this Structure

1AIE is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mittl PR, Chene P, Grutter MG. Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template. Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):86-9. PMID:9761820

Page seeded by OCA on Mon Feb 16 19:58:58 2009

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1aie

From Proteopedia

P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE

About this Structure

Reference

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