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

作者：Nishikawa Yoshimi; Takahara Yoshifumi; Asada Shinichi; Shigenaga Akira; Otaka Akira; Kitagawa Kouki; Koide Takaki^*

来源：Bioorganic & Medicinal Chemistry, 2010, 18(11): 3767-3775.

DOI：10.1016/j.bmc.2010.04.054

• Heat-shock protein 47 (HSP47)
• Chaperone
• Collagen
• Peptide

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.

• 出版日期2010-6-1