1tjf
From Proteopedia
The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation
Structural highlights
FunctionCAP_DICDI May have a regulatory bifunctional role. Binds G-actin and PIP2. Involved in microfilament reorganization near the plasma membrane in a PIP2-regulated manner. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCyclase-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 (N-CAP) 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 2.2 A resolution. The present crystal structure allows the characterization of a head-to-tail N-CAP dimer in the asymmetric unit and a crystallographic side-to-side 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. Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP).,Yusof AM, Hu NJ, Wlodawer A, Hofmann A Proteins. 2005 Feb 1;58(2):255-62. PMID:15558566[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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