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ADP-ribosyltransferases: plastic tools for inactivating protein and small molecular weight targets



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Koch-Nolte, Friedrich y Reche, Pedro A y Haag, Friedrich y Bazan, Fernando (2001) ADP-ribosyltransferases: plastic tools for inactivating protein and small molecular weight targets. Journal of Biotechnology, 92 (2). pp. 81-7. ISSN 1873-4863

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URL Oficial: http://www.elsevier.com/wps/find/journaldescription.cws_home/505515/description#description


ADP-ribosyltransferases (ADPRTs) form an interesting class of enzymes with well-established roles as potent bacterial toxins and metabolic regulators. ADPRTs catalyze the transfer of the ADP-ribose moiety from NAD(+) onto specific substrates including proteins. ADP-ribosylation usually inactivates the function of the target. ADPRTs have become adapted to function in extra- and intracellular settings. Regulation of ADPRT activity can be mediated by ligand binding to associated regulatory domains, proteolytic cleavage, disulphide bond reduction, and association with other proteins. Crystallisation has revealed a conserved core set of elements that define an unusual minimal scaffold of the catalytic domain with remarkably plastic sequence requirements--only a single glutamic acid residue critical to catalytic activity is invariant. These inherent properties of ADPRTs suggest that the ADPRT catalytic fold is an attractive, malleable subject for protein design.

Tipo de documento:Artículo
Palabras clave:ADP-ribosylation; Bacterial toxins; Amino acid sequence alignment; Sequence homology; Structure prediction; Protein design
Materias:Ciencias Biomédicas > Biología > Evolución
Ciencias > Informática > Bioinformática
Ciencias Biomédicas > Biología > Biología molecular
Código ID:9343
Depositado:17 Aug 2009 08:54
Última Modificación:03 Sep 2010 10:32

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