Syracuse

Low resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein.

Archive ouverte

Bernocco, S. | Steiglitz, Bm | Svergun, Di | Petoukhov, Mv | Ruggiero, Florence | Ricard-Blum, S. | Ebel, Christine | Geourjon, C. | Deleage, G. | Font, B. | Eichenberger, D. | Greenspan, Ds | Hulmes, Dj

Edité par CCSD ; American Society for Biochemistry and Molecular Biology -

International audience. Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that can stimulate the action of tolloid metalloproteinases, such as bone morphogenetic protein-1, on a procollagen substrate, by up to 20-fold. The PCPE molecule consists of two CUB domains followed by a C-terminal NTR (netrin-like) domain. In order to obtain structural insights into the function of PCPE, the recombinant protein was characterized by a range of biophysical techniques, including analytical ultracentrifugation, transmission electron microscopy, and small angle x-ray scattering. All three approaches showed PCPE to be a rod-like molecule, with a length of approximately 150 A. Homology modeling of both CUB domains and the NTR domain was consistent with the low-resolution structure of PCPE deduced from the small angle x-ray scattering data. Comparison with the low-resolution structure of the procollagen C-terminal region supports a recently proposed model (Ricard-Blum, S., Bernocco, S., Font, B., Moali, C., Eichenberger, D., Farjanel, J., Burchardt, E. R., van der Rest, M., Kessler, E., and Hulmes, D. J. S. (2002) J. Biol. Chem. 277, 33864-33869) for the mechanism of action of PCPE.

• Description
• Sujet/Public
• Outil
• Outil d'anticipation
• Mémoire et thèse
• Gestion