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dc.contributor.authorYusof, A.
dc.contributor.authorHofmann, A.
dc.contributor.editorRichard Perham (Editor-in-Chief
dc.description.abstractCyclase-associated protein (CAP) is a highly conserved and widely distributed protein required for normal cell growth and development. In yeast, CAP is a component of the adenylyl cyclase complex and helps to activate the Ras-mediated catalytic cycle of the cyclase. Full-length CAP constitutes an N-terminal domain (N-CAP), required for Ras response, a C-terminal domain (C-CAP), that interacts with the cytoskeleton, and a proline-rich middle domain, which can bind to SH3 domains. N-CAP and C-CAP have been shown to be dimeric in their crystal structures [1, 2]. Our own crystallographic studies on N-CAP from Dictyostelium discoideum [3, 4] have revealed the presence of both a head-to-tail dimer conformation, along with the previously reported side-to-side dimer [1]. These interactions are indicative of the variable modes of oligomerization, which makes studies on full-length CAP difficult to perform. We present the results of experiments to elucidate the oligomerization behaviour of CAP in solution and their comparison to findings from the crystal structures.
dc.publisherWiley-Blackwell Publishing Ltd.
dc.publisher.placeUnited Kingdom
dc.relation.ispartofconferencenameThe 30th FEBS Congress
dc.relation.ispartofconferencetitleThe 30th FEBS Congress
dc.relation.ispartoflocationBudapest, Hungary
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classified
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchMedical Biochemistry and Metabolomics
dc.titleStructural characterization of cyclase-associated protein (CAP) domains
dc.typeConference output
dc.type.descriptionE3 - Conferences (Extract Paper)
dc.type.codeE - Conference Publications
gro.rights.copyright© 2005 Economic Society of Australia QLD Inc. Published by Blackwell Publishing Ltd. Please refer to the publisher's website for access to the definitive, published version.
gro.hasfulltextNo Full Text
gro.griffith.authorHofmann, Andreas

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    Contains papers delivered by Griffith authors at national and international conferences.

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