Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Calcium transport across the sarcoplasmic reticulum - Structure and function of Ca2+-ATPase and the ryanodine receptor
Autore:
Stokes, DL; Wagenknecht, T;
Indirizzi:
NYU, Sch Med, Skirball Inst Biomol Med, New York, NY 10012 USA NYU New York NY USA 10012 kirball Inst Biomol Med, New York, NY 10012 USA NYU, Sch Med, Dept Cell Biol, New York, NY 10012 USA NYU New York NY USA 10012 Sch Med, Dept Cell Biol, New York, NY 10012 USA SUNY Albany, Wadsworth Ctr, Div Mol Med, Albany, NY 12222 USA SUNY AlbanyAlbany NY USA 12222 th Ctr, Div Mol Med, Albany, NY 12222 USA SUNY Albany, Dept Biomed Sci, Albany, NY USA SUNY Albany Albany NY USASUNY Albany, Dept Biomed Sci, Albany, NY USA
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 17, volume: 267, anno: 2000,
pagine: 5274 - 5279
SICI:
0014-2956(200009)267:17<5274:CTATSR>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
CA2+ RELEASE CHANNELS; P-TYPE ATPASE; SKELETAL-MUSCLE; CRYOELECTRON MICROSCOPY; MOLECULAR-IDENTIFICATION; ANGSTROM RESOLUTION; IMAGE-ANALYSIS; BINDING-SITE; H+-ATPASE; ION-PUMP;
Keywords:
Ca2+-ATPase; calcium transport; muscle; ryanodine receptor; sarcoplasmic reticulum;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Stokes, DL NYU, Sch Med, Skirball Inst Biomol Med, 540 1st Ave, New York, NY 10012 USA NYU 540 1st Ave New York NY USA 10012 e, New York, NY 10012 USA
Citazione:
D.L. Stokes e T. Wagenknecht, "Calcium transport across the sarcoplasmic reticulum - Structure and function of Ca2+-ATPase and the ryanodine receptor", EUR J BIOCH, 267(17), 2000, pp. 5274-5279

Abstract

Contraction of striated muscle results from a rise in cytoplasmic calcium concentration in a process termed excitation/contraction coupling. Most of this calcium moves back and forth across the sarcoplasmic-reticulum membrane in cycles of contraction and relaxation. The channel responsible for release from the sarcoplasmic reticulum is the ryanodine receptor, whereas Ca2+-ATPase effects reuptake in an ATP-dependent manner. The structures of these two molecules have been studied by cryoelectron microscopy, with helical crystals in the case of Ca2+-ATPase and as isolated tetramers in the case of ryanodine receptor. Structures of Ca2+-ATPase at 8-Angstrom resolution reveal the packing of transmembrane helices and have allowed fitting of a putative ATP-binding domain among the cytoplasmic densities. Comparison of ATPases in different conformations gives hints about the conformational changes that accompany the reaction cycle. Structures of ryanodine receptor at 30-Angstrom resolution reveal a multitude of isolated domains in the cytoplasmic portion, as well as a distinct transmembrane assembly. Binding sites for various protein ligands have been determined and conformational changes induced by ATP, calcium and ryanodine have been characterized. Both molecules appear to use large conformational changes to couple interactions in their cytoplasmic domains with calcium transport through their membrane domains, and future studies at higher resolution will focus on the mechanisms for this coupling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 11:00:24