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A ribbon diagram of the structure of the cPLA2 C2 domain, which is studied in the Falke group. The C2 domain exhibits a beta-sandwich architecture composed of two four-stranded, anti-parallel beta sheets (coordinates provided by Roger Williams and coworkers). In cytosolic phospholipase A2, docking to phosphatidylcholine headgroups is activated by the binding of two calcium ions to the C2 domain. The molecular basis of membrane docking is unknown, as are the mechanisms by which the calcium activation and headgroup specificity of the C2 motif are optimized for different pathways (Nalefski & Falke, 1996). (Collaborator: James Clark, Genetics Institute, Inc) |
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Nalefski, E.A., M.M. Slazas and J.J. Falke (1997) The calcium signaling cycle of a membrane-docking C2 domain. Biochemistry 36: 12011-12018
Nalefski, N.A., T. McDonagh, W. Somers, J. Seehra, J.J. Falke, and J.D. Clark (1998) Independent folding and ligand specificity of the C2 domain of cPLA2. J. Biol. Chem. 273: 1365-1372.
Nalefski, E.A. and J.J. Falke (1996) The C2 domain calcium binding motif: Structural and functional diversity. Protein Sci. 5: 2375-2390.