Structures of four Ca2+-bound troponin C at 2.0 Å resolution: further insights into the Ca2+-switch in the calmodulin superfamily
- 1 December 1997
- Vol. 5 (12) , 1695-1711
- https://doi.org/10.1016/s0969-2126(97)00315-8
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- A model of Ca2+-free calmodulin binding to unconventional myosins reveals how calmodulin acts as a regulatory switchStructure, 1996
- Structure of the regulatory domain of scallop myosin at 2 å resolution: implications for regulationStructure, 1996
- Calcium-induced conformational transition revealed by the solution structure of apo calmodulinNature Structural & Molecular Biology, 1995
- Structure of the regulatory domain of scallop myosin at 2.8 Ä resolutionNature, 1994
- Calmodulin structure refined at 1.7 Å resolutionJournal of Molecular Biology, 1992
- Molecular mechanism of troponin-C functionJournal of Muscle Research and Cell Motility, 1992
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Interaction of troponin I and troponin CJournal of Molecular Biology, 1991
- Refined crystal structure of troponin C from turkey skeletal muscle at 2·0 Å resolutionJournal of Molecular Biology, 1988
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977