期刊
JOURNAL OF BIOMOLECULAR NMR
卷 18, 期 3, 页码 217-227出版社
KLUWER ACADEMIC PUBL
DOI: 10.1023/A:1026563923774
关键词
calmodulin; dipolar coupling; heteronuclear NMR; homology model; liquid crystal; refinement
For an increasing fraction of proteins whose structures are being studied, sequence homology to known structures permits building of low resolution structural models. It is demonstrated that dipolar couplings, measured in a liquid crystalline medium, not only can validate such structural models, but also refine them. Here, experimental H-1-N-15, H-1(alpha)-C-13(alpha), and C-13'-C-13(alpha) dipolar couplings are shown to decrease the backbone rmsd between various homology models of calmodulin (CaM) and its crystal structure. Starting from a model of the Ca2+-saturated C-terminal domain of CaM, built from the structure of Ca2+-free recoverin on the basis of remote sequence homology, dipolar couplings are used to decrease the rmsd between the model and the crystal structure from 5.0 to 1.25 Angstrom. A better starting model, built from the crystal structure of Ca2+-saturated parvalbumin, decreases in rmsd from 1.25 to 0.93 Angstrom. Similarly, starting from the structure of the Ca2+-ligated CaM N-terminal domain, experimental dipolar couplings measured for the Ca2+-free form decrease the backbone rmsd relative to the refined solution structure of apo-CaM from 4.2 to 1.0 Angstrom.
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