Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Structure of the TPR domain of p67(phox) in complex with Rac center dot GTP
Autore:
Lapouge, K; Smith, SJM; Walker, PA; Gamblin, SJ; Smerdon, SJ; Rittinger, K;
Indirizzi:
Natl Inst Med Res, Div Prot Struct, London NW7 1AA, England Natl Inst Med Res London England NW7 1AA Struct, London NW7 1AA, England
Titolo Testata:
MOLECULAR CELL
fascicolo: 4, volume: 6, anno: 2000,
pagine: 899 - 907
SICI:
1097-2765(200010)6:4<899:SOTTDO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHRONIC GRANULOMATOUS-DISEASE; NADPH OXIDASE ACTIVATION; RESPIRATORY BURST OXIDASE; PROTEIN-PROTEIN INTERACTIONS; TETRATRICOPEPTIDE REPEAT; CRYSTAL-STRUCTURE; TARGET PROTEINS; EFFECTOR REGION; BINDING DOMAIN; INSERT REGION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Rittinger, K Natl Inst Med Res, Div Prot Struct, Mill Hill, London NW7 1AA, England Natl Inst Med Res Mill Hill London England NW7 1AA , England
Citazione:
K. Lapouge et al., "Structure of the TPR domain of p67(phox) in complex with Rac center dot GTP", MOL CELL, 6(4), 2000, pp. 899-907

Abstract

p67(phox) is an essential part of the NADPH oxidase, a multiprotein enzymecomplex that produces superoxide ions in response to microbial infection. Binding of the small GTPase Rac to p67(phox) is a key step in the assembly of the active enzyme complex. The structure of Rac GTP bound to the N-terminal TPR (tetratricopeptide repeat) domain of p67(phox) reveals a novel modeof Rho family/effector interaction and explains the basis of GTPase specificity. Complex formation is largely mediated by an insertion between two TPR motifs, suggesting an unsuspected versatility of TPR domains in target recognition and in their more general role as scaffolds for the assembly of multiprotein complexes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 20:59:00