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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase

Article Abstract:

AspRS belongs to class II aminoacyl-RNA synthetases whose crystal structure is known, and have been cocrystallized with their cognate tRNA. The refined crystal structure of AspRS complexes with tRNAAsp was obtained at 2.9 Angstrom resolution. The data reveal three regions of contact, each involving a domain of AspRS and at least one identity determinant of tRNAAsp. Furthermore, the findings suggest that the mode of binding of the acceptor stem of tRNAAsp by AspRS can be generalized to class II aminoacyl-tRNA synthetases.

Author: Rees, Bernard, Moras, Dino, Cavarelli, Jean, Ruff, Marc, Thierry, Jean-Claude
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
Yeast, Yeast (Food product), Transfer RNA, Ligases

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Structural basis for messenger RNA movement on the ribosome

Article Abstract:

The mRNA structure upstream of the Shine-Dalgarno (SD) helix in the initiation complex was studied by comparing the X-ray structures of eight ribosome complexes modelling the translation initiation, post-initiation and elongation states. After the initiation of translation but while an SD interaction is still present, mRNA moves in the 3'->5' direction with simultaneous clockwise rotation and lengthening of the SD duplex bringing it into contact with ribosomal protein S2.

Author: Rees, Bernard, Moras, Dino, Yusupova, Gulnara, Jenner, Lasse, Yusupov, Marat
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
France, Science & research, Analysis, Genetic aspects, Gram-negative bacteria, Ribosomes, Messenger RNA, Crystallization, X-ray analysis

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Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

Article Abstract:

The structure of ligand-activated factors has been further elucidated by a new study which characterized the crystal structure of the ligand-binding domain (LBD) of the human receptor RXR-alpha for 9-cis retinoic acid. The results reveal a fold of antiparallel alpha-helical sandwich arranged as dimeric units. The stereochemical interactions of the LBD structure with various ligands are described.

Author: Chambon, Pierre, Moras, Dino, Gronemeyer, Hinrich, Ruff, Marc, Bourguet, William
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
Genetic regulation, Genetic transcription, Transcription (Genetics), Ligand binding (Biochemistry)

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