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Titolo:
Electron cryomicroscopy and bioinformatics suggest protein fold models forrice dwarf virus
Autore:
Zhou, ZH; Baker, ML; Jiang, W; Dougherty, M; Jakana, J; Dong, G; Lu, GY; Chiu, W;
Indirizzi:
Baylor Coll Med, Program Struct & Computat Biol & Mol Biophys, Houston, TX77030 USA Baylor Coll Med Houston TX USA 77030 & Mol Biophys, Houston, TX77030 USA Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Natl Ctr Macromol Imaging, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030romol Imaging, Houston, TX 77030 USA Univ Texas, Sch Med, Dept Pathol & Lab Med, Houston, TX 77030 USA Univ Texas Houston TX USA 77030 t Pathol & Lab Med, Houston, TX 77030 USA Beijing Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Genet Engn, Beijing 100871, Peoples R China Beijing Univ Beijing Peoples R China 100871 jing 100871, Peoples R China
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 10, volume: 8, anno: 2001,
pagine: 868 - 873
SICI:
1072-8368(200110)8:10<868:ECABSP>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
STRUCTURE PREDICTION; CORE; CRYSTALLOGRAPHY; VISUALIZATION; PHYTOREOVIRUS; RESOLUTION; ANGSTROM; SERVER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Chiu, W Baylor Coll Med, Program Struct & Computat Biol & Mol Biophys, Houston, TX77030 USA Baylor Coll Med Houston TX USA 77030 iophys, Houston, TX77030 USA
Citazione:
Z.H. Zhou et al., "Electron cryomicroscopy and bioinformatics suggest protein fold models forrice dwarf virus", NAT ST BIOL, 8(10), 2001, pp. 868-873

Abstract

The three-dimensional structure of rice dwarf virus was determined to 6.8 Angstrom resolution by single particle electron cryomicroscopy. By integrating the structural analysis with bioinformatics, the folds of the proteins in the double-shelled capsid were derived. In the outer shell protein, the uniquely orientated upper and lower domains are composed of similar secondary structure elements but have different relative orientations from that ofbluetongue virus in the same Reoviridae family. Differences in both sequence and structure between these proteins may be important in defining virus-host interactions. The inner shell protein adopts a conformation similar toother members of Reoviridae, suggesting a common ancestor that has evolvedto infect hosts ranging from plants to animals. Symmetry mismatch between the two shells results in nonequivalent, yet specific, interactions that contribute to the stability of this large macromolecular machine.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 00:58:28