Modulation of quaternary structure of S100 proteins by calcium ions.
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ABSTRACT:
SUBMITTER: Streicher WW
PROVIDER: S-EPMC2926197 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Publications
Modulation of quaternary structure of S100 proteins by calcium ions.
Streicher Werner W WW Lopez Maria M MM Makhatadze George I GI
Biophysical chemistry 20100623 3
It is well established that calcium binding leads to conformational changes in S100 proteins. These conformational changes are thought to activate the protein and render a protein conformation that is capable of binding other proteins. The basic quaternary structural motif of S100 proteins is a homodimer, however there is little information if higher order non-covalent oligomers are also formed and whether these oligomers are of functional relevance. To this end we performed equilibrium analytic ...[more]
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