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 | |
| Publication status | Published - 2010 Jun 1 |
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Keywords
- Chaperone
- Collagen
- Heat-shock protein 47 (HSP47)
- Peptide
ASJC Scopus subject areas
- Pharmaceutical Science
- Drug Discovery
- Organic Chemistry
- Molecular Medicine
- Molecular Biology
- Clinical Biochemistry
- Biochemistry
Cite this
A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47. / Nishikawa, Yoshimi; Takahara, Yoshifumi; Asada, Shinichi; Shigenaga, Akira; Otaka, Akira; Kitagawa, Kouki; Koide, Takaki.
In: Bioorganic and Medicinal Chemistry, Vol. 18, No. 11, 01.06.2010, p. 3767-3775.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47
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.
KW - Chaperone
KW - Collagen
KW - Heat-shock protein 47 (HSP47)
KW - Peptide
UR - http://www.scopus.com/inward/record.url?scp=77953138390&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77953138390&partnerID=8YFLogxK
U2 - 10.1016/j.bmc.2010.04.054
DO - 10.1016/j.bmc.2010.04.054
M3 - Article
VL - 18
SP - 3767
EP - 3775
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
SN - 0968-0896
IS - 11
ER -