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The structure of calsequestrin, the major calcium-binding protein of skeletal muscle sarcoplasmic reticulum, consists of three thioredoxin folds that condense to form an acidic platform for calcium adsorption.
The crystal structure of a T cell receptor bound to a self peptide–major histocompatibility complex antigen reveals poor shape complementarity in the interface between the two proteins, as well as large conformational changes in the T cell receptor combining site upon ligand binding.
Structures of two short-lived intermediates during the photocycle of the photoactive yellow protein (PYP) have been determined using X-ray crystallography. These structures demonstrate the power of cryo-trapping and the Laue method in trapping transient intermediates.
New results indicate that a K+ channel switches from a closed state to an open state by widening the hydrophobic pore on the cytoplasmic side of the membrane.
