Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation |
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Authors: | KJ Edwards DL Ollis NE Dixon |
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Affiliation: | Department of Biomedical Sciences, School of Public Health and Wadsworth Center, New York State Department of Health, Albany, NY 12201-0509, USA. Terry@orkney.ph.albany.edu |
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Abstract: | Ryanodine receptors (RyRs), a class of intracellular calcium release channels, are the largest ion channels known. Recently, cryoelectron microscopy and image reconstructions of isolated receptors have shown that most of the protein mass forms a porous, multidomain cytoplasmic assembly. Evidence is mounting that suggests that the cytoplasmic assembly communicates with the transmembrane regions over distances of 100 or greater. RyRs are centrally important in excitation-contraction coupling, which occurs at specialized regions where the sarcoplasmic reticulum, containing the RyRs, and the plasma membrane/transverse-tubule system form junctions. Numerous proteins are present at these junctions, some of which interact directly with the RyR. |
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