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

研究成果: Article査読

14 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)3767-3775
ページ数9
ジャーナルBioorganic and Medicinal Chemistry
18
11
DOI
出版ステータスPublished - 2010 6 1

ASJC Scopus subject areas

  • 生化学
  • 分子医療
  • 分子生物学
  • 薬科学
  • 創薬
  • 臨床生化学
  • 有機化学

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