Specific recognition of the collagen triple helix by chaperone HSP47: minimal structural requirement and spatial molecular orientation
T Koide, S Asada, Y Takahara, Y Nishikawa… - Journal of Biological …, 2006 - jbc.org
The unique folding of procollagens in the endoplasmic reticulum is achieved with the
assistance of procollagen-specific molecular chaperones. Heat-shock protein 47 (HSP47) is
an endoplasmic reticulum-resident chaperone that plays an essential role in normal
procollagen folding, although its molecular function has not yet been clarified. Recent
advances in studies on the binding specificity of HSP47 have revealed that Arg residues at
Yaa positions in collagenous Gly-Xaa-Yaa repeats are critical for its interactions (Koide, T …
assistance of procollagen-specific molecular chaperones. Heat-shock protein 47 (HSP47) is
an endoplasmic reticulum-resident chaperone that plays an essential role in normal
procollagen folding, although its molecular function has not yet been clarified. Recent
advances in studies on the binding specificity of HSP47 have revealed that Arg residues at
Yaa positions in collagenous Gly-Xaa-Yaa repeats are critical for its interactions (Koide, T …
