The linker of calmodulin--to helix or not to helix.
The linker regions of the central helices of calmodulin and of troponin C are observed to be alpha-helices in crystal and in solution. However, these linkers are predicted to be non-helical by standard algorithms. Further, there is strong evidence that when calmodulin interacts with some of its targets this linker helix bends. The linker appears to be delicately balanced between helical and non-helical conformations. A review of this subject suggests that one can anticipate more unpredicted conformations for the central helices of the score of other proteins that have four EF-hand domains.
Kretsinger
R H
RH
Department of Biology, University of Virginia, Charlottesville.
D000595:Amino Acid Sequence; D002147:Calmodulin / Q000737:chemistry*; D003460:Crystallization; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014336:Troponin / Q000737:chemistry*; D019209:Troponin C
D002147:Calmodulin; D014336:Troponin; D019209:Troponin C