Collagen molecular chaperon

Stress protein molecular chaperones have already been introduced (see Chapter 6). Such proteins have a rich and varied molecular recognition and binding behaviour. Important examples include GroEL and the procollagen/collagen molecular chaperone protein known as heat shock protein 47 (Hsp47). 

Nagata, K. (1996) Hsp47 a collagen-specific molecular chaperone. Trends in Biochemical Sciences 21, 23-26. 

Koide, T., Takahara, Y., Asada, S., and Nagata, K. (2002). Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47. /. Biol. Chem. 277, 6178-6182. 

Nagata K. Expression and function of heat shock protein 47 a collagen-specific molecular chaperone in the endoplasmic reticulum. Matrix Biology 1998, 16, 379-386. 

Tasab, M. Jenkinson, L. Bullcid, N.J. Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47. J. Biol. Chem. 2002. 277 (38). 35007-35012. 

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