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Título

Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily

AutorGomis-Rüth, F. Xavier CSIC ORCID ; Companys, Verònica; Qian, Y.; Fricker, Lloyd D.; Vendrell, Josep; Avilés, Francesc X.; Coll, Miquel CSIC ORCID
Palabras claveCarboxypeptidase
Inhibitor design
Metalloprotease
Transthyretin
X-ray crystal structure
Fecha de publicación1-nov-1999
EditorNature Publishing Group
CitaciónEMBO Journal 18(21):5817-5826 (1999)
ResumenThe 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 similarity to and general coincidence of the key catalytic residues with the archetypal pancreatic carboxypeptidase 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/bhydrolase subdomain is followed by a C-terminal 80 residue b-sandwich subdomain, unique for these regulatory 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 modelling of regulatory carboxypeptidases as well as a more rational design of inhibitors of carboxypeptidase D.
Descripción10 pages, 4 figures, 1 table.-- PMID: 10545093 [PubMed].-- PMCID: PMC1171647.
Versión del editorhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171647
URIhttp://hdl.handle.net/10261/31250
ISSN0261-4189
E-ISSN1460-2075
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