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A configuration space of homologous proteins conserving mutual information and allowing a phylogeny inference based on pair-wise Z-score probabilities Inra
Bastien, O.; Ortet, P.; Roy, S.; Maréchal, E..
Tipo: Journal Article Palavras-chave: PROTEINE HOMOLOGUE; SEQUENCE PROTEIQUE; ALIGNEMENT DE SEQUENCES; METHODE AUTOMATIQUE; PROBABILITE.
Ano: 2005 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0500032104110132&uri=/notices/prodinra1/2007/09/
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A multiple alignment of the capside protein sequences of nepoviruses and comoviruses suggests a common structure Inra
Le Gall; Candresse, T.; Dunez, J..
The amino acid sequences of the regions encoding the structural proteins of eleven nepoviruses and five comoviruses, two genera of the familyComoviridae, have been aligned. The properties predicted by computer analysis (three-dimensional-3D-structure, hydrophobicity) are also correlated along this alignment, and aligned to the experimentally determined 3D structure of two comoviruses. It can thus be assumed that the 3D structure of the unique nepovirus coat protein matches that of the bipartite protomer found in the comovirus particles. In this model, the spatial locations of two amino-acid motifs characteristic of nepoviruses are in close vicinity, at the external surface of the virion. The coat proteins of nepoviruses and comoviruses may thus share a...
Tipo: Journal Article Palavras-chave: CCMV; VIRUS DES MARBRURES CHLOROTIQUES DU VIGNA; PROTEINE DE CAPSIDE; PHYTOVIRUS; VIRUS DE PLANTE; STRUCTURE TRI DIMENSIONNELLE; ALIGNEMENT DE SEQUENCES; SEQUENCE; BROMOVIRUS.
Ano: 1995 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB9600010949053125&uri=/notices/prodinra1/2010/11/
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