Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity.

@article{Blanc2007InsightsIH,
  title={Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity.},
  author={Guillaume Blanc and Bernard Font and Denise Eichenberger and Christophe J. Moreau and Sylvie Ricard-Blum and David J S Hulmes and Catherine Moali},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 23},
  pages={16924-33}
}
Procollagen C-proteinase enhancers (PCPE-1 and -2) are extracellular glycoproteins that can stimulate the C-terminal processing of fibrillar procollagens by tolloid proteinases such as bone morphogenetic protein-1. They consist of two CUB domains (CUB1 and -2) that alone account for PCPE-enhancing activity and one C-terminal NTR domain. CUB domains are found in several extracellular and plasma membrane-associated proteins, many of which are proteases. We have modeled the structure of the CUB1… CONTINUE READING