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Bioorg Med Chem. 2010 Jun 1;18(11):3767-75. doi: 10.1016/j.bmc.2010.04.054. Epub 2010 Apr 21.

A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47.

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Department of Chemistry and Biochemistry, Waseda University, Tokyo 169-8555, Japan.


Heat-shock protein 47 (HSP47) is a chaperone that facilitates the proper folding of procollagen. Our previous studies showed that the high-affinity HSP47-binding motif in the collagen triple helix is Xaa-(Thr/Pro)-Gly-Xaa-Arg-Gly. In this study, we further investigated structural requirements for the HSP47-binding motif, using synthetic triple-helical collagen-model peptides with systematic amino acid substitutions at either the Thr/Pro (=Yaa(-3)) or the Arg (=Yaa(0)) position. Results obtained from in vitro binding assays indicated that HSP47 detects the side-chain structure of Arg at the Yaa(0)-position, while the Yaa(-3) amino acid serves as the secondary recognition site that affects affinity to HSP47.

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