Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activitiy. II: Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment
- Author
- FLAHERTY, K. M; WILBANKS, S. M; DELUCA-FLAHERTY, C; MCKAY, D. B
Stanford univ. school medicine, dep. cell biology, Beckman Laboratories for Structural Biology, Stanford CA 94305, United States - Source
The Journal of biological chemistry (Print). 1994, Vol 269, Num 17, pp 12899-12907 ; ref : 22 ref
- CODEN
- JBCHA3
- ISSN
- 0021-9258
- Scientific domain
- Biochemistry, molecular biology, biophysics; Biotechnology
- Publisher
- American Society for Biochemistry and Molecular Biology, Bethesda, MD
- Publication country
- United States
- Document type
- Article
- Language
- English
- Keyword (fr)
- Activité enzymatique Adenosinetriphosphatase Bovin Diffraction RX Fixation ligand Mécanisme action Protéine choc thermique Structure 3 dimensions Chaperone Protéine Hsc70 Artiodactyla Enzyme Hydrolases Mammalia Ungulata Vertebrata
- Keyword (en)
- Enzymatic activity Adenosinetriphosphatase Bovine X ray diffraction Ligand binding Mechanism of action Heat shock protein Spatial structure Chaperone Artiodactyla Enzyme Hydrolases Mammalia Ungulata Vertebrata
- Keyword (es)
- Actividad enzimática Adenosinetriphosphatase Bovino Difracción RX Fijación ligando Mecanismo acción Proteína choque térmico Estructura 3 dimensiones Artiodactyla Enzima Hydrolases Mammalia Ungulata Vertebrata
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02D Proteins / 002A02D08 Binding and carrier proteins
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02E Enzymes and enzyme inhibitors / 002A02E04 Hydrolases
- Discipline
- Analytical, structural and metabolic biochemistry
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 4153819
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1016/S0021-9258(18)99961-8 
https://dx.doi.org/10.1016/S0021-9258(18)99961-8
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