Organization of polar groups of 9 kd calbindin around Ca2+ ions bound to the protein: a microdielectric study.
Using a simple model of linear response of polarizable centers to an electric field, function delta is defined to characterize structural organization of protein polar groups. The function makes it possible to detect specific structures of nonuniformly distributed and mutually coupled groups that can transmit local structural and charge density perturbations, induced by an ion over long distances to functionally active sites of a protein molecule. In 9 kd calbinding (a small protein from the troponin C superfamily) two structural chains have been demonstrated that link together both Ca2+ ions coordinated by the protein. The chains form a rigid structure stabilized by coordination of one of the ions, so that binding of the other is promoted. Such a structure is probably common to all members of the superfamily and plays an important role in the mechanism of calcium binding by these proteins.
Wesołowski
T A
TA
University of Warsaw, Department of Biophysics, Poland.
Boguta
G
G
Bierzyński
A
A
D001665:Binding Sites; D064026:Calbindins; D002118:Calcium / Q000737:chemistry* / Q000378:metabolism; D004574:Electromagnetic Fields; D008433:Mathematics; D012044:Regression Analysis; D064030:S100 Calcium Binding Protein G / Q000737:chemistry* / Q000378:metabolism
D064026:Calbindins; D064030:S100 Calcium Binding Protein G; D002118:Calcium