The predicted structure of the calcium-binding component of troponin.
作者： Robert H. Kretsinger , C.David Barry
DOI: 10.1016/0005-2795(75)90312-8
关键词: EF hand 、 Crystallography 、 Component (thermodynamics) 、 Calcium 、 Chemistry 、 Parvalbumin 、 Tropomyosin binding 、 Lanthanide 、 Side chain 、 Troponin
摘要: The structure prediction of the calcium binding component troponin (TN-C) incorporates following assumptions: (1) TN-C contains four regions homologous to “EF hand” parvalbumin. (2) EF hands are arranged in two pairs with overall symmetry, 222. (3) which not connect within each pair, one and three four, pairs, region three. In resulting model there is a well-defined hydrophobic core made from side chains all eight helical loops. Ca2+ separated by 11 A; while another over 30 A. Cys-98 Tyr-109 suggested be sensitive spectroscopic probes. Calcium(1) solvent accessible most readily replaced lanthanide. Because symmetry troponin, can anticipate that inhibitory- tropomyosin components similar another.
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