2012年8月1日
Crystallization and X-ray diffraction analysis of the ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment involved in translesion DNA synthesis.
Acta crystallographica. Section F, Structural biology and crystallization communications
- ,
- ,
- ,
- ,
- 巻
- 68
- 号
- Pt 8
- 開始ページ
- 962
- 終了ページ
- 4
- 記述言語
- 英語
- 掲載種別
- 研究論文（学術雑誌）
- DOI
- 10.1107/S1744309112032435
- 出版者・発行元
- WILEY-BLACKWELL
REV1, REV3 and REV7 are pivotal proteins in translesion DNA synthesis that allows DNA synthesis to continue even in the presence of DNA damage. REV1 and REV3 are error-prone DNA polymerases, while REV7 acts as an adaptor protein that links them together. A ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment has been crystallized. The crystals belonged to space group P3(1)21, with unit-cell parameters a = b = 74.7, c = 124.5 Å.
- リンク情報
-
- DOI
- https://doi.org/10.1107/S1744309112032435
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/22869133
- PubMed Central
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412784
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000307217700026&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1107/S1744309112032435
- ISSN : 1744-3091
- PubMed ID : 22869133
- PubMed Central 記事ID : PMC3412784
- Web of Science ID : WOS:000307217700026