| http://purl.uniprot.org/citations/33589610 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33589610 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33589610 | http://www.w3.org/2000/01/rdf-schema#comment | "Upon binding to DNA breaks, poly(ADP-ribose) polymerase 1 (PARP1) ADP-ribosylates itself and other factors to initiate DNA repair. Serine is the major residue for ADP-ribosylation upon DNA damage, which strictly depends on HPF1. Here, we report the crystal structures of human HPF1/PARP1-CAT ΔHD complex at 1.98 Å resolution, and mouse and human HPF1 at 1.71 Å and 1.57 Å resolution, respectively. Our structures and mutagenesis data confirm that the structural insights obtained in a recent HPF1/PARP2 study by Suskiewicz et al. apply to PARP1. Moreover, we quantitatively characterize the key residues necessary for HPF1/PARP1 binding. Our data show that through salt-bridging to Glu284/Asp286, Arg239 positions Glu284 to catalyze serine ADP-ribosylation, maintains the local conformation of HPF1 to limit PARP1 automodification, and facilitates HPF1/PARP1 binding by neutralizing the negative charge of Glu284. These findings, along with the high-resolution structural data, may facilitate drug discovery targeting PARP1."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-021-21302-4"xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-021-21302-4"xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Zhang N."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Zhang N."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Zhao P."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Zhao P."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Yun C.H."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Yun C.H."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Kong L.L."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Kong L.L."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Sun F.H."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Sun F.H."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Wong C.C.L."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/author | "Wong C.C.L."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/pages | "1028"xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/pages | "1028"xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/title | "HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones."xsd:string |
| http://purl.uniprot.org/citations/33589610 | http://purl.uniprot.org/core/title | "HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones."xsd:string |