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

Yoshimi Nishikawa, Yoshifumi Takahara, Shinichi Asada, Akira Shigenaga, Akira Otaka, Kouki Kitagawa, Takaki Koide

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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 (=Yaa0) position. Results obtained from in vitro binding assays indicated that HSP47 detects the side-chain structure of Arg at the Yaa0-position, while the Yaa-3 amino acid serves as the secondary recognition site that affects affinity to HSP47.

Original languageEnglish
Pages (from-to)3767-3775
Number of pages9
JournalBioorganic and Medicinal Chemistry
Volume18
Issue number11
DOIs
Publication statusPublished - 2010 Jun 1

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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