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Crystallization and preliminary X-ray crystallographic analysis of the N domain of p97/VCP in complex with the UBX domain of FAF1.

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dc.contributor.authorShin, HY-
dc.contributor.authorKang, W-
dc.contributor.authorLee, SY-
dc.contributor.authorYang, JK-
dc.date.accessioned2011-05-31T05:18:10Z-
dc.date.available2011-05-31T05:18:10Z-
dc.date.issued2010-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/2755-
dc.description.abstractp97/VCP is a multifunctional AAA(+)-family ATPase that is involved in diverse cellular processes. p97/VCP directly interacts with various adaptors for activity in different biochemical contexts. Among these adaptors are p47 and Fas-associated factor 1 (FAF1), which contain a common UBX domain through which they bind to the N domain of p97/VCP. In the ubiquitin-proteasome pathway, p97/VCP acts as a chaperone that presents client proteins to the proteasome for degradation, while FAF1 modulates the process by interacting with ubiquitinated client proteins and also with p97/VCP. In an effort to elucidate the structural details of the interaction between p97/VCP and FAF1, the p97/VCP N domain was crystallized in complex with the FAF1 UBX domain. X-ray data were collected to 2.60 A resolution and the crystals belonged to space group C222(1), with unit-cell parameters a = 58.24, b = 72.81, c = 132.93 A. The Matthews coefficient and solvent content were estimated to be 2.39 A(3) Da(-1) and 48.4%, respectively, assuming that the asymmetric unit contained p97/VCP N domain and FAF1 molecules in a 1:1 ratio, which was subsequently confirmed by molecular-replacement calculations.-
dc.language.isoen-
dc.subject.MESHAdaptor Proteins, Signal Transducing-
dc.subject.MESHAdenosine Triphosphatases-
dc.subject.MESHCell Cycle Proteins-
dc.subject.MESHCrystallization-
dc.subject.MESHCrystallography, X-Ray-
dc.subject.MESHHumans-
dc.subject.MESHProtein Structure, Tertiary-
dc.titleCrystallization and preliminary X-ray crystallographic analysis of the N domain of p97/VCP in complex with the UBX domain of FAF1.-
dc.typeArticle-
dc.identifier.pmid20057067-
dc.identifier.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2805533/-
dc.contributor.affiliatedAuthor이, 상윤-
dc.type.localJournal Papers-
dc.identifier.doi10.1107/S1744309109047691-
dc.citation.titleActa crystallographica. Section F, Structural biology and crystallization communications-
dc.citation.volume66-
dc.citation.numberPt1-
dc.citation.date2010-
dc.citation.startPage41-
dc.citation.endPage43-
dc.identifier.bibliographicCitationActa crystallographica. Section F, Structural biology and crystallization communications, 66(Pt1). : 41-43, 2010-
dc.identifier.eissn1744-3091-
dc.relation.journalidJ017443091-
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Journal Papers > Research Organization > Institute for Medical Sciences
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