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1oqa

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This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1oqa, 15 NMR models ()

Gene:

BRCA1 (Homo sapiens)

Domains:

BRCT

Related:

1jnx, 1kzy, 1cdz

Structural annotation:
Resources:	CATH : 1Oqaa00 InterPro : Ipr013083, Ipr011364, Ipr002378, Ipr001357, Ipr001841 Pfam : PF00533 SCOP : d1oqaa_ UniProt : P38398

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

1 Solution structure of the BRCT-c domain from human BRCA1
2 Disease
3 About this Structure
4 Reference

Solution structure of the BRCT-c domain from human BRCA1

Publication Abstract from PubMed

BRCA1 is a tumor suppressor protein associated with breast and ovarian cancer. The C-terminal region of BRCA1 consists of two closely spaced BRCT domains which mediate essential biological functions, including regulation of transcription and control of cell-cycle progression by their interaction with phosphorylated effector proteins. Here we report the NMR structure of the isolated C-terminal BRCT domain (BRCT-c) from human BRCA1. BRCT-c is well-structured in solution, folding independently in the absence of its BRCT-n counterpart. Ultracentrifugation experiments and size exclusion chromatography reveal that BRCT-c exists as a monomer under near-physiological conditions. Dynamics measurements from NMR data show three loops which coincide with the most variable sequence regions in BRCT domains, to be genuinely flexible in solution. The solution structure of BRCT-c shows subtle conformational changes when compared to the crystal structure of BRCT-c in the tandem repeat of BRCA1. These affect sites involved in formation of the BRCT-n-BRCT-c interface and the binding to phosphoserine-containing peptides. The results suggest that the presence of native BRCT-n and a properly aligned BRCT-n-BRCT-c interface are essential if BRCT-c is to adopt a biologically active conformation. Structural consequences of cancer-associated mutations and biological implications of the dynamic behavior are discussed.

Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1., Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U, Biochemistry. 2004 Dec 28;43(51):15983-95. PMID:15609993

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

Disease

Known disease associated with this structure: Breast cancer-1 OMIM:[113705], Breast-ovarian cancer OMIM:[113705], Ovarian cancer OMIM:[113705], Papillary serous carcinoma of the peritoneum OMIM:[113705]

About this Structure

1OQA is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U. Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1. Biochemistry. 2004 Dec 28;43(51):15983-95. PMID:15609993 doi:10.1021/bi049550q

Page seeded by OCA on Tue Feb 17 06:27:16 2009

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1oqa

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Contents

Solution structure of the BRCT-c domain from human BRCA1

Disease

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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