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Titolo:
Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity
Autore:
Menetrey, J; Macia, E; Pasqualato, S; Franco, M; Cherfils, J;
Indirizzi:
CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France CNRS Gif Sur Yvette France F-91198 truct, F-91198 Gif Sur Yvette, France CNRS, Inst Pharmacol Mol & Cellulaire, F-06560 Valbonne, France CNRS Valbonne France F-06560 Mol & Cellulaire, F-06560 Valbonne, France
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 6, volume: 7, anno: 2000,
pagine: 466 - 469
SICI:
1072-8368(200006)7:6<466:SOASAB>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADP-RIBOSYLATION FACTOR-6; MAMMALIAN-CELLS; PLASMA-MEMBRANE; SEC7 DOMAIN; PROTEIN; GDP; ARF; ACTIVATION; REARRANGEMENTS; TRAFFICKING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Cherfils, J CNRS, Lab Enzymol & Biochim Struct, Ave de la Terrasse, F-91198 Gif Sur Yvette, France CNRS Ave de la Terrasse Gif Sur Yvette France F-91198 France
Citazione:
J. Menetrey et al., "Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity", NAT ST BIOL, 7(6), 2000, pp. 466-469

Abstract

Arf6 is an isoform of Arf that localizes at the periphery of the cell where it has an essential role in endocytotic pathways. Its function does not overlap with that of Arf1, although the two proteins share similar to 70% sequence identity and they have switch regions, whose conformation depends onthe nature of the guanine nucleotide, with almost identical sequences. Thecrystal structure of Arf6-GDP at 2.3 Angstrom shows that it has a conformation similar to that of Arf1-GDP, which cannot bind membranes with high affinity. Significantly, the switch regions of Arf6 deviate by 2-5 Angstrom from those of Arf1. These differences are a consequence of the shorter N-terminal linker of Arf6 and of discrete sequence changes between Arf6 and Arf1. Mutational analysis shows that one of the positions which differs between Arf1 and Arf6 affects the configuration of the nucleotide binding site and thus the nucleotide binding properties of the Arf variant Altogether, our results provide a structural basis for understanding how Arf1 and Arf6 can be distinguished by their guanine nucleotide exchange factors and suggest a model for the nudeotide/membrane cycle of Arf6.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 07:25:16