-
Three-dimensional structure of calmodulin.
The three-dimensional structure of calmodulin has been determined crystallographically at 3.0 A resolution. The molecule consists of two globular lobes connected by a long exposed alpha-helix. Each lobe binds two calcium ions through helix-loop-helix domains similar to those of other calcium-binding proteins. The long helix between the lobes may be involved in interactions of calmodulin with drugs and various proteins.
PMID: 3990807 [PubMed - indexed for MEDLINE]
-
Cited by 67 PubMed Central articles
-
N- and C-terminal domains of the calcium binding protein EhCaBP1 of the parasite Entamoeba histolytica display distinct functions.
Jain R, Kumar S, Gourinath S, Bhattacharya S, Bhattacharya A.
PLoS One. 2009; 4(4):e5269. Epub 2009 Apr 22.
[PLoS One. 2009]
-
An allosteric model of calmodulin explains differential activation of PP2B and CaMKII.
Stefan MI, Edelstein SJ, Le Novère N.
Proc Natl Acad Sci U S A. 2008 Aug 5; 105(31):10768-73. Epub 2008 Jul 31.
[Proc Natl Acad Sci U S A. 2008]
-
Thermodynamics of calmodulin binding to cardiac and skeletal muscle ryanodine receptor ion channels.
Meissner G, Pasek DA, Yamaguchi N, Ramachandran S, Dokholyan NV, Tripathy A.
Proteins. 2009 Jan; 74(1):207-11.
[Proteins. 2009]
- » See all...
Structures reported by this article