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1n0w

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1n0w, resolution 1.70Å ()

Ligands:

, ,

Non-Standard Residues:

Gene:

RAD51 (Homo sapiens), BRCA2 (Homo sapiens)

Domains:

Rad51_DMC1_radA, Rad51, BRCA2

Structural annotation:
Resources:	CATH : 1N0Wa00 InterPro : Ipr001553, Ipr003583, Ipr013632, Ipr003593, Ipr011941, Ipr010995, Ipr015188, Ipr015205, Ipr015187, Ipr015252, Ipr015525, Ipr002093, Ipr011370 Pfam : PF08423, PF00634 SCOP : d1n0wa_, d1n0wb_ UniProt : Q06609, P51587

Functional annotation:
Resources:	GeneCard : RAD51, BRCA2
Cellular component:	intracellular condensed nuclear chromosome condensed chromosome nucleus cytoplasm protein complex secretory granule centrosome BRCA2-MAGE-D1 complex
Biological process:	DNA metabolic process meiotic recombination response to DNA damage stimulus DNA recombination protein homooligomerization double-strand break repair via homologous recombination meiosis mitotic recombination DNA repair positive regulation of DNA ligation DNA unwinding during replication regulation of transcription, DNA-dependent nucleotide-excision repair response to estrogen stimulus cytokinesis during cell cycle centrosome duplication double-strand break repair negative regulation of mammary gland epithelial cell proliferation response to genistein regulation of S phase of mitotic cell cycle multi-organism process
Molecular function:	identical protein binding sequence-specific DNA binding single-stranded DNA binding protein C-terminus binding DNA binding nucleoside-triphosphatase activity double-stranded DNA binding ATPase activity DNA-dependent ATPase activity damaged DNA binding recombinase activity ATP binding protein binding nucleotide binding single-stranded DNA-dependent ATPase activity histone acetyltransferase activity transcription activator activity gamma-tubulin 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 Crystal structure of a RAD51-BRCA2 BRC repeat complex
2 Disease
3 About this Structure
4 Reference

Crystal structure of a RAD51-BRCA2 BRC repeat complex

Publication Abstract from PubMed

The breast cancer susceptibility protein BRCA2 controls the function of RAD51, a recombinase enzyme, in pathways for DNA repair by homologous recombination. We report here the structure of a complex between an evolutionarily conserved sequence in BRCA2 (the BRC repeat) and the RecA-homology domain of RAD51. The BRC repeat mimics a motif in RAD51 that serves as an interface for oligomerization between individual RAD51 monomers, thus enabling BRCA2 to control the assembly of the RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. The RAD51 oligomerization motif is highly conserved among RecA-like recombinases, highlighting a common evolutionary origin for the mechanism of nucleoprotein filament formation, mirrored in the BRC repeat. Cancer-associated mutations that affect the BRC repeat disrupt its predicted interaction with RAD51, yielding structural insight into mechanisms for cancer susceptibility.

Insights into DNA recombination from the structure of a RAD51-BRCA2 complex., Pellegrini L, Yu DS, Lo T, Anand S, Lee M, Blundell TL, Venkitaraman AR, Nature. 2002 Nov 21;420(6913):287-93. Epub 2002 Nov 10. PMID:12442171

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

Disease

Known disease associated with this structure: Breast cancer 2, early onset OMIM:[600185], Fanconi anemia, complementation group D1 OMIM:[600185], Pancreatic cancer OMIM:[600185], Prostate cancer OMIM:[600185], Wilms tumor OMIM:[600185], Breast cancer, male, susceptibility to OMIM:[600185], Glioblastoma OMIM:[600185], Medulloblastoma OMIM:[600185], Pre-B-cell acute lymphoblastic leukemia , OMIM:[600185]

About this Structure

1N0W is a 4 chains structure of sequences from [1] and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Pellegrini L, Yu DS, Lo T, Anand S, Lee M, Blundell TL, Venkitaraman AR. Insights into DNA recombination from the structure of a RAD51-BRCA2 complex. Nature. 2002 Nov 21;420(6913):287-93. Epub 2002 Nov 10. PMID:12442171 doi:10.1038/nature01230

Page seeded by OCA on Tue Feb 17 21:47:47 2009

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1n0w

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Contents

Crystal structure of a RAD51-BRCA2 BRC repeat complex

Disease

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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