Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.
Sung, Nuri
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Mar 2016 - 2952-7 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
1091-6490
10.1073/pnas.1516167113 doi
Adenosine Triphosphate--chemistry
Allosteric Regulation
Allosteric Site
Amino Acid Motifs
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding Sites
Computer Simulation
Crystallography, X-Ray
HSP70 Heat-Shock Proteins--metabolism
HSP90 Heat-Shock Proteins--chemistry
Humans
Mitochondria--metabolism
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
Protein Folding
Rabbits
Recombinant Fusion Proteins--chemistry
Sequence Homology, Amino Acid
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Mar 2016 - 2952-7 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
1091-6490
10.1073/pnas.1516167113 doi
Adenosine Triphosphate--chemistry
Allosteric Regulation
Allosteric Site
Amino Acid Motifs
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding Sites
Computer Simulation
Crystallography, X-Ray
HSP70 Heat-Shock Proteins--metabolism
HSP90 Heat-Shock Proteins--chemistry
Humans
Mitochondria--metabolism
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
Protein Folding
Rabbits
Recombinant Fusion Proteins--chemistry
Sequence Homology, Amino Acid