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1t29

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1t29, resolution 2.30Å ()

Non-Standard Residues:

Domains:

BRCT

Structural annotation:
Resources:	CATH : 1T29A01, 1T29A02 InterPro : Ipr013083, Ipr002378, Ipr001357, Ipr011364, Ipr001841, Ipr010614, Ipr014001, Ipr002464, Ipr006555, Ipr013020, Ipr014013 Pfam : PF00533 SCOP : d1t29a2, d1t29a1 UniProt : P38398, Q9BX63

Functional annotation:
Resources:	GeneCard : BRCA1
Cellular component:	protein complex gamma-tubulin ring complex ubiquitin ligase complex nucleus intracellular BRCA1-BARD1 complex cytoplasm
Biological process:	DNA repair DNA damage response, signal transduction resulting in induction of apoptosis androgen receptor signaling pathway fatty acid biosynthetic process lipid biosynthetic process response to estrogen stimulus positive regulation of transcription, DNA-dependent negative regulation of transcription DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator regulation of DNA repair positive regulation of DNA repair response to DNA damage stimulus double-strand break repair via homologous recombination chromosome segregation cell cycle negative regulation of cell cycle regulation of cell proliferation positive regulation of protein ubiquitination protein ubiquitination postreplication repair regulation of apoptosis regulation of transcription from RNA polymerase III promoter negative regulation of fatty acid biosynthetic process regulation of transcription from RNA polymerase II promoter apoptosis negative regulation of centriole replication nucleobase, nucleoside, nucleotide and nucleic acid metabolic process double-strand break repair DNA damage checkpoint
Molecular function:	protein binding transcription coactivator activity transcription activator activity DNA binding androgen receptor binding enzyme binding ubiquitin-protein ligase activity zinc ion binding tubulin binding metal ion binding nucleic acid binding ATP binding hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ATP-dependent helicase activity ATP-dependent DNA helicase activity hydrolase activity nucleotide binding helicase activity

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

Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide

Publication Abstract from PubMed

The recognition of the phosphorylated BACH1 helicase by the BRCA1 C-terminal (BRCT) repeats is important to the tumor suppressor function of BRCA1. Here we report the crystal structure of the BRCT repeats of human BRCA1 bound to a phosphorylated BACH1 peptide at 2.3 A resolution. The phosphorylated serine 990 and phenylalanine 993 of BACH1 anchor the binding to BRCA1 through specific interactions with a surface cleft at the junction of the two BRCT repeats. This surface cleft is highly conserved in BRCA1 across species, suggesting an evolutionarily conserved function of phosphopeptide recognition. Importantly, conserved amino acids critical for BACH1 binding are frequently targeted for missense mutations in breast cancer. These mutations greatly diminish the ability of BRCA1 to interact with the phosphorylated BACH1 peptide. Additional structural analysis revealed significant implications for understanding the function of the BRCT family of proteins in DNA damage and repair signaling.

Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling., Shiozaki EN, Gu L, Yan N, Shi Y, Mol Cell. 2004 May 7;14(3):405-12. PMID:15125843

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

About this Structure

1T29 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Shiozaki EN, Gu L, Yan N, Shi Y. Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling. Mol Cell. 2004 May 7;14(3):405-12. PMID:15125843

Page seeded by OCA on Tue Feb 17 23:49:45 2009

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1t29

From Proteopedia

Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide

About this Structure

Reference

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