A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47.
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.
Nishikawa
Yoshimi
Y
Department of Chemistry and Biochemistry, Waseda University, Tokyo 169-8555, Japan.
Takahara
Yoshifumi
Y
Asada
Shinichi
S
Shigenaga
Akira
A
Otaka
Akira
A
Kitagawa
Kouki
K
Koide
Takaki
T
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003094:Collagen / Q000378:metabolism*; D050958:HSP47 Heat-Shock Proteins / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D013329:Structure-Activity Relationship
D050958:HSP47 Heat-Shock Proteins; D003094:Collagen