The three-dimensional structure of Ca2+-bound calcyclin: implications for Ca2+-signal transduction by S100 proteins
Open Access
- 1 February 1998
- Vol. 6 (2) , 223-231
- https://doi.org/10.1016/s0969-2126(98)00023-9
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- The solution structure of the bovine S100B protein dimer in the calcium-free stateStructure, 1996
- Solution Structure of Rat Apo-S100B(ββ) As Determined by NMR Spectroscopy,Biochemistry, 1996
- Solution structure of calcium-free calmodulinNature Structural & Molecular Biology, 1995
- Structures of the troponin C regulatory domains in the apo and calcium-saturated statesNature Structural & Molecular Biology, 1995
- Calcium-induced structural changes and domain autonomy in calmodulinNature Structural & Molecular Biology, 1995
- Calcium-induced conformational transition revealed by the solution structure of apo calmodulinNature Structural & Molecular Biology, 1995
- The structure of calcyclin reveals a novel homodimeric fold for S100 Ca2+-binding proteinsNature Structural & Molecular Biology, 1995
- Modulation of Calmodulin Plasticity in Molecular Recognition on the Basis of X-Ray StructuresScience, 1993
- Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide ComplexScience, 1992
- Solution structure of a calmodulin-target peptide complex by multidimensional NMRScience, 1992