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Titolo:
Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments
Autore:
Djinovic-Carugo, K; Young, P; Gautel, M; Saraste, M;
Indirizzi:
European Mol Biol Lab, Struct Biol Programme, D-69012 Heidelberg, Germany European Mol Biol Lab Heidelberg Germany D-69012 012 Heidelberg, Germany
Titolo Testata:
CELL
fascicolo: 4, volume: 98, anno: 1999,
pagine: 537 - 546
SICI:
0092-8674(19990820)98:4<537:SOTARM>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPECTRIN-LIKE REPEATS; MAXIMUM-LIKELIHOOD; CYTOPLASMIC DOMAIN; DIFFRACTION DATA; COILED-COIL; ION-PAIRS; PROTEIN; ASSOCIATION; ALIGNMENT; ADHESION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Saraste, M European Mol Biol Lab, Struct Biol Programme, Postfach 10-2209,D-69012 Heidelberg, Germany European Mol Biol Lab Postfach 10-2209 Heidelberg Germany D-69012
Citazione:
K. Djinovic-Carugo et al., "Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments", CELL, 98(4), 1999, pp. 537-546

Abstract

We have determined the crystal structure of the two central repeats in thealpha-actinin rod at 2.5 Angstrom resolution. The repeats are connected bya helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which revealsthe structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 21:13:19