-
Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures.
Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.
Calmodulin is the primary calcium-dependent signal transducer and regulator of a wide variety of essential cellular functions. The structure of calcium-calmodulin bound to the peptide corresponding to the calmodulin-binding domain of brain calmodulin-dependent protein kinase II alpha was determined to 2 angstrom resolution. A comparison to two other calcium-calmodulin structures reveals how the central helix unwinds in order to position the two domains optimally in the recognition of different target enzymes and clarifies the role of calcium in maintaining recognition-competent domain structures.
PMID: 8259515 [PubMed - indexed for MEDLINE]
-
Cited by 63 PubMed Central articles
-
CaMKIIbeta binding to stable F-actin in vivo regulates F-actin filament stability.
Lin YC, Redmond L.
Proc Natl Acad Sci U S A. 2008 Oct 14; 105(41):15791-6. Epub 2008 Oct 7.
[Proc Natl Acad Sci U S A. 2008]
-
The unfoldomics decade: an update on intrinsically disordered proteins.
Dunker AK, Oldfield CJ, Meng J, Romero P, Yang JY, Chen JW, Vacic V, Obradovic Z, Uversky VN.
BMC Genomics. 2008 Sep 16; 9 Suppl 2:S1. Epub 2008 Sep 16.
[BMC Genomics. 2008]
-
Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently.
Guo Q, Jureller JE, Warren JT, Solomaha E, Florián J, Tang WJ.
J Biol Chem. 2008 Aug 29; 283(35):23836-45. Epub 2008 Jun 26.
[J Biol Chem. 2008]
- » See all...
Structures reported by this article