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dc.contributor.authorYusof, AM
dc.contributor.authorHu, NJ
dc.contributor.authorWlodawer, A
dc.contributor.authorHofmann, A
dc.date.accessioned2017-05-03T15:19:09Z
dc.date.available2017-05-03T15:19:09Z
dc.date.issued2005
dc.date.modified2008-02-14T08:18:35Z
dc.identifier.issn0887-3585
dc.identifier.urihttp://hdl.handle.net/10072/16740
dc.description.abstractCyclase-associated protein (CAP) is a highly conserved and widely distributed protein that links the nutritional response signaling to cytoskeleton remodeling. In yeast, CAP is a component of the adenylyl cyclase complex and helps to activate the Ras-mediated catalytic cycle of the cyclase. While the N-terminal domain of CAP (NCAP) provides a binding site for adenylyl cyclase, the C-terminal domain (C-CAP) possesses actin binding activity. Our attempts to crystallize full-length recombinant CAP from Dictyostelium discoideum resulted in growth of orthorhombic crystals containing only the N-terminal domain (residues 42-227) due to auto-proteolytic cleavage. The structure was solved by molecular replacement with data at 2.2A͊resolution. The present crystal structure allows the characterization of a head-to-tail N-CAP dimer in the asymmetric unit and a crystallographic side-toside dimer. Comparison with previously published structures of N-CAP reveals variable modes of dimerization of this domain, but the presence of a common interface for the side-to-side dimer.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherWILEY-LISS, INC.
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom255
dc.relation.ispartofpageto262
dc.relation.ispartofjournalProteins: Structure, Function, and Bioinformatics
dc.relation.ispartofvolume58
dc.rights.retentionY
dc.subject.fieldofresearchMathematical sciences
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchInformation and computing sciences
dc.subject.fieldofresearchcode49
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode46
dc.titleStructural Evidence for Variable Oligomerization of the N-Terminal Domain of Cyclase-Associated Protein (CAP)
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2005
gro.hasfulltextNo Full Text
gro.griffith.authorHofmann, Andreas


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