Calcium-free Calmodulin

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Contents

Calcium-free Calmodulin

General Information


Calmodulin is a molecule that has been studied extensively in its functions within the cell, and has an important role in relaying Ca2+ signals within the cytosol. [1] It does this by binding to Ca2+, undergoing a conformational change, and may interact with various proteins within the cell.[1][2][3] Once bound to a target protein, it undergoes a further conformational change and may activate certain systems. For example, there is a Ca2+ pump in the plasma membrane pump that is activated by the binding of Ca2+-bound calmodulin, and then uses ATP to drive the Ca2+ out of the cell. [4]

Calcium-bound Calmodulin

The structure of calcium-bound calmodulin had previously been discovered using x-ray crystallography [3]. It was then theorized that knowledge of the structure of calcium-free calmodulin would give greater insight into the function of the protein. Attempts were made to crystallize the calcium-free (or apo) form,


PDB ID 1cfc

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1cfc, 25 NMR models ()
Related: 1cfd
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml







References

  1. 1.0 1.1 Hoeflich, K.P., & Ikura, M.. Calmodulin in action: diversity in target recognition and activation mechanisms, Cell. 2002 108:739-742
  2. Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. Nat Struct Biol. 1995 Sep;2(9):768-76. PMID:7552748
  3. 3.0 3.1 Babu YS, Bugg CE, Cook WJ. Structure of calmodulin refined at 2.2 A resolution. J Mol Biol. 1988 Nov 5;204(1):191-204. PMID:3145979
  4. Berridge MJ, Bootman MD, Roderick HL. Calcium signalling: dynamics, homeostasis and remodelling. Nat Rev Mol Cell Biol. 2003 Jul;4(7):517-29. PMID:12838335 doi:10.1038/nrm1155
  • Babu YS, Bugg CE, Cook WJ. Structure of calmodulin refined at 2.2 A resolution. J Mol Biol. 1988 Nov 5;204(1):191-204. PMID:3145979
  • Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. Nat Struct Biol. 1995 Sep;2(9):768-76. PMID:7552748
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