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| {{STRUCTURE_1tjf| PDB=1tjf | SCENE= }} | | {{STRUCTURE_1tjf| PDB=1tjf | SCENE= }} |
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| '''The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation'''
| | ===The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation=== |
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| ==Overview==
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| Cyclase-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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15558566}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15558566 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15558566}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Yusof, A Mohd.]] | | [[Category: Yusof, A Mohd.]] |
| [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:01:09 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:50:05 2008'' |
