Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이공주 | - |
dc.date.accessioned | 2016-08-28T12:08:30Z | - |
dc.date.available | 2016-08-28T12:08:30Z | - |
dc.date.issued | 2009 | - |
dc.identifier.issn | 0961-8368 | - |
dc.identifier.other | OAK-6032 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/220333 | - |
dc.description.abstract | Fas-associated factor (FAF)-1 is a multidomain protein that was first identified as a member of the Fas death-inducing signaling complex, but later found to be involved in various biological processes. Although the exact mechanisms are not clear, FAF1 seems to play an important role in cancer, asbestos-induced mesotheliomas, and Parkinson's disease. It interacts with polyubiquitinated proteins, Hsp70, and p97/VCP (valosin-containing protein), in addition to the proteins of the Fas-signaling pathway. We have determined the crystal structure of the ubiquitin-associated domain of human FAF1 (hFAF1-UBA) and examined its interaction with ubiquitin and ubiquitin-like proteins using nuclear magnetic resonance. hFAF1-UBA revealed a canonical three-helical bundle that selectively binds to mono- and di-ubiquitin (Lys48-linked), but not to SUMO-1 (small ubiquitin-related modifier 1) or NEDD8 (neural precursor cell expressed, developmentally down-regulated 8). The interaction between hFAF1-UBA and di-ubiquitin involves hydrophobic interaction accompanied by a transition in the di-ubiquitin conformation. These results provide structural insight into the mechanism of polyubiquitin recognition by hFAF1-UBA. Published by Wiley-Blackwell. © 2009 The Protein Society. | - |
dc.language | English | - |
dc.title | Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1 | - |
dc.type | Article | - |
dc.relation.issue | 11 | - |
dc.relation.volume | 18 | - |
dc.relation.index | SCI | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.startpage | 2265 | - |
dc.relation.lastpage | 2276 | - |
dc.relation.journaltitle | Protein Science | - |
dc.identifier.doi | 10.1002/pro.237 | - |
dc.identifier.wosid | WOS:000271518100007 | - |
dc.identifier.scopusid | 2-s2.0-70350511436 | - |
dc.author.google | Song J. | - |
dc.author.google | Joon K.P. | - |
dc.author.google | Lee J.-J. | - |
dc.author.google | Choi Y.-S. | - |
dc.author.google | Ryu K.-S. | - |
dc.author.google | Kim J.-H. | - |
dc.author.google | Kim E. | - |
dc.author.google | Lee K.-J. | - |
dc.author.google | Jeon Y.-H. | - |
dc.author.google | Kim E.E. | - |
dc.contributor.scopusid | 이공주(7501497635;57191532162) | - |
dc.date.modifydate | 20230208115507 | - |