Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.

  title={Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.},
  author={Guennadi Kozlov and Sara Bastos-Aristizabal and Pekka M{\"a}{\"a}tt{\"a}nen and Angelika Rosenauer and Fenglin Zheng and April Killikelly and Jean-François Trempe and David Y. Thomas and Kalle Gehring},
  journal={The Journal of biological chemistry},
  volume={285 46},
Little is known about how chaperones in the endoplasmic reticulum are organized into complexes to assist in the proper folding of secreted proteins. One notable exception is the complex of ERp57 and calnexin that functions as part the calnexin cycle to direct disulfide bond formation in N-glycoproteins. Here, we report three new complexes composed of the peptidyl prolyl cis-trans-isomerase cyclophilin B and any of the lectin chaperones: calnexin, calreticulin, or calmegin. The 1.7 Å crystal… CONTINUE READING
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