Title : Structure and calcium-binding studies of a recoverin mutant (E85Q) in an allosteric intermediate state.

Pub. Date : 2002 May 7

PMID : 11980481






7 Functional Relationships(s)
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1 Structure and calcium-binding studies of a recoverin mutant (E85Q) in an allosteric intermediate state. Calcium recoverin Homo sapiens
2 Recoverin, a member of the EF-hand superfamily, serves as a calcium sensor in retinal rod cells. Calcium recoverin Homo sapiens
3 Previous structural studies revealed that the myristoyl group of recoverin is sequestered inside the protein core in the absence of calcium. Calcium recoverin Homo sapiens
4 The cooperative binding of two calcium ions to the second and third EF-hands (EF-2 and EF-3) of recoverin leads to the extrusion of the fatty acid. Calcium recoverin Homo sapiens
5 The cooperative binding of two calcium ions to the second and third EF-hands (EF-2 and EF-3) of recoverin leads to the extrusion of the fatty acid. Fatty Acids recoverin Homo sapiens
6 Here we present nuclear magnetic resonance (NMR), fluorescence, and calcium-binding studies of a myristoylated recoverin mutant (myr-E85Q) designed to abolish high-affinity calcium binding to EF-2 and thereby trap the myristoylated protein with calcium bound solely to EF-3. Calcium recoverin Homo sapiens
7 Here we present nuclear magnetic resonance (NMR), fluorescence, and calcium-binding studies of a myristoylated recoverin mutant (myr-E85Q) designed to abolish high-affinity calcium binding to EF-2 and thereby trap the myristoylated protein with calcium bound solely to EF-3. Calcium recoverin Homo sapiens