5FOW
HUMANISED MONOMERIC RADA IN COMPLEX WITH WHTA TETRAPEPTIDE
Summary for 5FOW
| Entry DOI | 10.2210/pdb5fow/pdb |
| Related | 5FOS 5FOT 5FOU 5FOV 5FOX |
| Descriptor | DNA repair and recombination protein RadA, WHTA PEPTIDE, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, rada, fxxa motif, recombinase |
| Biological source | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) More |
| Total number of polymer chains | 4 |
| Total formula weight | 52271.44 |
| Authors | Scott, D.E.,Marsh, M.,Blundell, T.L.,Abell, C.,Hyvonen, M. (deposition date: 2015-11-26, release date: 2016-03-30, Last modification date: 2024-01-10) |
| Primary citation | Scott, D.E.,Marsh, M.,Blundell, T.L.,Abell, C.,Hyvonen, M. Structure Activity Relationship of the Peptide Binding Motif Mediating the Rad51:Brca2 Protein-Protein Interaction. FEBS Lett., 590:1094-, 2016 Cited by PubMed Abstract: 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. PubMed: 26992456DOI: 10.1002/1873-3468.12139 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.797 Å) |
Structure validation
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