Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/26325
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen |
Autor: | García Sáez, Isabel; Reverter, David; Vendrell, Josep; Avilés, Francesc X.; Coll, Miquel CSIC ORCID | Palabras clave: | Activation Carboxypeptidase A2 Inhibition Pro-enzyme Three-dimensional structure |
Fecha de publicación: | dic-1997 | Editor: | Nature Publishing Group | Citación: | EMBO Journal 16(23):6906-6913 (1997) | Resumen: | The three-dimensional structure of human procarboxypeptidase A2 has been determined using X-ray crystallography at 1.8 A resolution. This is the first detailed structural report of a human pancreatic carboxypeptidase and of its zymogen. Human procarboxypeptidase A2 is formed by a pro-segment of 96 residues, which inhibits the enzyme, and a carboxypeptidase moiety of 305 residues. The pro-enzyme maintains the general fold when compared with other non-human counterparts. The globular part of the pro-segment docks into the enzyme moiety and shields the S2-S4 substrate binding sites, promoting inhibition. Interestingly, important differences are found in the pro-segment which allow the identification of the structural determinants of the diverse activation behaviours of procarboxypeptidases A1, B and A2, particularly of the latter. The benzylsuccinic inhibitor is able to diffuse into the active site of procarboxypeptidase A2 in the crystals. The structure of the zymogen-inhibitor complex has been solved at 2.2 A resolution. The inhibitor enters the active site through a channel formed at the interface between the pro-segment and the enzyme regions and interacts with important elements of the active site. The derived structural features explain the intrinsic activity of A1/A2 pro-enzymes for small substrates. | Descripción: | 8 pages, 4 figures, 3 tables.-- PMID: 9384570 [PubMed].-- PMCID: PMC1170294. | Versión del editor: | http://dx.doi.org/10.1093/emboj/16.23.6906 | URI: | http://hdl.handle.net/10261/26325 | DOI: | 10.1093/emboj/16.23.6906 | ISSN: | 0261-4189 | E-ISSN: | 1460-2075 |
Aparece en las colecciones: | (IQAC) Artículos |
Mostrar el registro completo
CORE Recommender
PubMed Central
Citations
25
checked on 10-abr-2024
SCOPUSTM
Citations
92
checked on 16-abr-2024
WEB OF SCIENCETM
Citations
89
checked on 23-feb-2024
Page view(s)
327
checked on 23-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.