English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/107809
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 65 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family

Autor Gomis-Rüth, F. Xavier ; Bayés, Àlex; Sotiropoulou, Georgia; Pampalakis, Georgios; Tsetsenis, Theodoros; Villegas, Sandra; Avilés, Francesc X.; Coll, Miquel
Palabras clave Proteins
Tumors
Extrapolation
Enzymes
Diseases
Biomarkers
Fecha de publicación jul-2002
EditorAmerican Society for Biochemistry and Molecular Biology
Citación Journal of Biological Chemistry 277(30): 27273-27281 (2002)
ResumenZyme/protease M/neurosin/human kallikrein 6 (hK6) is a member of the human kallikrein family of trypsin-like serine proteinases and was originally identified as being down-regulated in metastatic breast and ovarian tumors when compared with corresponding primary tumors. Recent evidence suggests that hK6 may serve as a circulating tumor marker in ovarian cancers. In addition, it was described in the brain of Parkinson's disease and Alzheimer's disease patients, where it is implicated in amyloid precursor protein processing. It is thus a biomarker for these diseases. To examine the mechanism of activation of hK6, we have solved the structure of its proform, the first of a human kallikrein family member. The proenzyme displays a fold that exhibits chimeric features between those of trypsinogen and other family members. It lacks the characteristic >kallikrein loop> and forms the six disulfide bridges of trypsin. Pro-hK6 displays a completely closed specificity pocket and a unique conformation of the regions involved in structural rearrangements upon proteolytic cleavage activation. This points to a novel activation mechanism, which could be extrapolated to other human kallikreins.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M201534200
URI http://hdl.handle.net/10261/107809
DOI10.1074/jbc.M201534200
Identificadoresdoi: 10.1074/jbc.M201534200
issn: 0021-9258
Aparece en las colecciones: (IBMB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.