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• W4255519797 abstract "Abstract Parvalbumin was the first EF‐hand protein to have been characterized and to have its crystal structure determined. This prototype consists of an α‐helix E (extended forefinger of a clenched right hand), loop around the Ca 2+ ion (clenched middle finger), and α‐helix F (extended thumb). Parvalbumin has provided a reference point for the analyses of 76 other subfamilies of proteins that contain 2 to 12 EF‐hands. Most, but not all, EF‐hands bind calcium. The Ca 2+ ion is almost always coordinated by seven oxygen atoms arranged in an approximate pentagonal bipyramid; usually one of the ligands is a carboxylate group that coordinates calcium with both its oxygen atoms. The affinities of EF‐hands for calcium range from p K d (Ca 2+ ) 6 to 8. The dissociation constant of parvalbumin for calcium ( K d ∼ 10 −8 M) reflects one of the highest affinities of all the EF‐hand proteins. All, or most, of the EF‐hand proteins bind calcium ∼10 4.0 more strongly than they bind the six‐coordinate magnesium. Most of this difference in affinity derives from the ∼10 3.4 greater on rate for calcium, which in turn derives from its faster dehydration rate. Parvalbumin functions in fast, white, skeletal muscle to soak up messenger calcium following a stimulus, thereby facilitating rapid relaxation. Whether it has an analogous function in neurons, thymus, or other tissues remains to be demonstrated. Most EF‐hand proteins change conformation upon binding calcium, thereby transducing the information content of a pulse of cytosolic messenger Ca 2+ ions. Although the binding of calcium to the two EF‐hands of monomeric parvalbumin is not (or only very weakly) cooperative, as is the case for other EF‐hand proteins, the interaction of a pair of EF‐hands is essential for the stability of these proteins. The angle between the two helices (E and F) of a single EF‐hand as well as the contact between the pair of EF‐hands is usually more open following binding of calcium, thereby exposing hydrophobic side chains. However, a survey of the known structures of all known EF‐hands proteins does not reveal a bimodal closed, open set of conformations reflecting either binding of calcium and/or binding of targets for those EF‐hand proteins involved in information transduction." @default.
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• W4255519797 date "2004-03-05" @default.
• W4255519797 modified "2023-09-29" @default.
• W4255519797 title "Parvalbumin" @default.
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• W4255519797 doi "https://doi.org/10.1002/0470028637.met043" @default.
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