2LE0
PARP BRCT Domain
Summary for 2LE0
Entry DOI | 10.2210/pdb2le0/pdb |
NMR Information | BMRB: 17687 |
Descriptor | Poly [ADP-ribose] polymerase 1 (1 entity in total) |
Functional Keywords | transferase |
Biological source | Rattus norvegicus (rat) |
Cellular location | Nucleus (By similarity): P27008 |
Total number of polymer chains | 1 |
Total formula weight | 11672.60 |
Authors | Mueller, G.,Loeffler, P.,Cuneo, M.,Derose, E.,London, R. (deposition date: 2011-06-03, release date: 2011-10-19, Last modification date: 2024-05-15) |
Primary citation | Loeffler, P.A.,Cuneo, M.J.,Mueller, G.A.,Derose, E.F.,Gabel, S.A.,London, R.E. Structural studies of the PARP-1 BRCT domain. Bmc Struct.Biol., 11:37-37, 2011 Cited by PubMed Abstract: Poly(ADP-ribose) polymerase-1 (PARP-1) is one of the first proteins localized to foci of DNA damage. Upon activation by encountering nicked DNA, the PARP-1 mediated trans-poly(ADP-ribosyl)ation of DNA binding proteins occurs, facilitating access and accumulation of DNA repair factors. PARP-1 also auto-(ADP-ribosyl)ates its central BRCT-containing domain forming part of an interaction site for the DNA repair scaffolding protein X-ray cross complementing group 1 protein (XRCC1). The co-localization of XRCC1, as well as bound DNA repair factors, to sites of DNA damage is important for cell survival and genomic integrity. PubMed: 21967661DOI: 10.1186/1472-6807-11-37 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
Download full validation report