| Autor: |
Gomis-Rüth, F. X., Companys, V., Qian, Y., Fricker, L. D., Vendrell, J., Avilés, F. X., Coll, M. |
| Předmět: |
|
| Zdroj: |
EMBO Journal; 11/1/99, Vol. 18 Issue 21, p5817-5826, 10p |
| Abstrakt: |
The crystal structure of domain II of duck carboxypeptidase D, a prohormone/propeptide processing enzyme integrated in a three repeat tandem in the natural system, has been solved, constituting a prototype for members of the regulatory metallocarboxypeptidase subfamily. It displays a 300 residue N-terminal ??a/??b-hydrolase subdomain with overall topological sim- ilarity to and general coincidence of the key catalytic residues with the archetypal pancreatic carboxypeptid- ase A. However, numerous significant insertions/deletions in segments forming the funnel-like access to the active site explain differences in specificity towards larger protein substrates or inhibitors. This ??a/??b- hydrolase subdomain is followed by a C-terminal 80 residue ??b-sandwich subdomain, unique for these regu- latory metalloenzymes and topologically related to transthyretin and sugar-binding proteins. The structure described here establishes the fundamentals for a better understanding of the mechanism ruling events such as prohormone processing and will enable model- ling of regulatory carboxypeptidases as well as a more rational design of inhibitors of carboxypeptidase D. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Plný text