Structural highlights
5fov is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , |
| Related: | 5fos, 5fot, 5fou, 5fow, 5fox |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[RADA_PYRFU] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules.
Publication Abstract from PubMed
RAD51 is a recombinase involved in the homologous recombination of double-strand breaks in DNA. RAD51 forms oligomers by binding to another molecule of RAD51 via an 'FxxA' motif, and the same recognition sequence is similarly utilised to bind BRCA2. We have tabulated the effects of mutation of this sequence, across a variety of experimental methods and from relevant mutations observed in the clinic. We use mutants of a tetrapeptide sequence to probe the binding interaction, using both isothermal titration calorimetry and X-ray crystallography. Where possible, comparison between our tetrapeptide mutational study and the previously reported mutations is made, discrepancies are discussed and the importance of secondary structure in interpreting alanine scanning and mutational data of this nature is considered.
Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction.,Scott DE, Marsh M, Blundell TL, Abell C, Hyvonen M FEBS Lett. 2016 Apr;590(8):1094-102. doi: 10.1002/1873-3468.12139. Epub 2016 Apr , 6. PMID:26992456[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Scott DE, Marsh M, Blundell TL, Abell C, Hyvonen M. Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction. FEBS Lett. 2016 Apr;590(8):1094-102. doi: 10.1002/1873-3468.12139. Epub 2016 Apr , 6. PMID:26992456 doi:http://dx.doi.org/10.1002/1873-3468.12139
