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

doi:10.1016/j.bmc.2010.04.054

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^*

^*Corresponding author for this work

School of Advanced Science and Engineering

Research output: Contribution to journal › Article › peer-review

16 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 language	English
Pages (from-to)	3767-3775
Number of pages	9
Journal	Bioorganic and Medicinal Chemistry
Volume	18
Issue number	11
DOIs	https://doi.org/10.1016/j.bmc.2010.04.054
Publication status	Published - 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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10.1016/j.bmc.2010.04.054

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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.",

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author = "Yoshimi Nishikawa and Yoshifumi Takahara and Shinichi Asada and Akira Shigenaga and Akira Otaka and Kouki Kitagawa and Takaki Koide",

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AU - Nishikawa, Yoshimi

AU - Takahara, Yoshifumi

AU - Asada, Shinichi

AU - Shigenaga, Akira

AU - Otaka, Akira

AU - Kitagawa, Kouki

AU - Koide, Takaki

PY - 2010/6/1

Y1 - 2010/6/1

N2 - 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.

AB - 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.

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KW - Heat-shock protein 47 (HSP47)

KW - Peptide

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

Abstract

Keywords

ASJC Scopus subject areas

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