scholarly journals Serine/threonine phosphorylation of calmodulin modulates its interaction with the binding domains of target enzymes

1999 ◽  
Vol 344 (2) ◽  
pp. 403-411 ◽  
Author(s):  
Estelle LECLERC ◽  
Chantal CORTI ◽  
Holger SCHMID ◽  
Stefan VETTER ◽  
Peter JAMES ◽  
...  
Keyword(s):  
Dissociation Constant ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Camp Phosphodiesterase ◽  
Calmodulin Binding ◽  
Binding Domains ◽  
Order Of Magnitude ◽  
Oxide Synthase ◽  
Muscle Myosin

The interaction of serine/threonine-phosphorylated calmodulin with synthetic peptides corresponding to the calmodulin-binding domains of six enzymes has been studied by fluorescence spectroscopy. For five peptides, the dissociation constant of the calmodulin-peptide complex (Kd) increased when calmodulin was phosphorylated. An increase of more than one order of magnitude was observed with peptides derived from smooth-muscle myosin light-chain kinase and cAMP phosphodiesterase. In contrast, only a slight increase in Kd was noted with two peptides derived from the plasma membrane Ca2+-ATPase and for the peptide derived from nitric oxide synthase. No significant change in affinity was detected with the peptide derived from calcineurin. In contrast, a decrease in the dissociation constant was observed with the peptide derived from the Ca2+-calmodulin dependent kinase II. Phosphorylation also affected the peptide-calmodulin binding stoichiometry: a decrease from two to one binding sites was observed with the peptides derived from myosin light-chain kinase and phosphodiesterase.

Three-dimensional structure of the complex between calmodulin mutant lacking the c-terminal five residues and the calmodulin-binding peptide derived from skeletal muscle myosin light-chain kinase

2017 ◽  
Vol 39 (3) ◽  
pp. 309-319
Author(s):  
Vu Van Dung ◽  
Yoshitaka Umetsu ◽  
Shinya Ohki
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Skeletal Muscle Myosin ◽  
Three Dimensional Structure ◽  
Calmodulin Binding ◽  
Muscle Myosin

In our previous study, functional ability and conformational stability had been examined for C-terminal deletion mutants of a 148-residue Ca2+-binding protein, chicken calmodulin (CaM). In that study, we had reported that a mutant named CCMΔ5, missing five residues at the C-terminus, activates CaM-target as much as full-length CaM does. This finding is intriguing because CCMΔ5 lacks the key residues, Met144 and Met145, for the target activation. To uncover why CCMΔ5 displays proper function, here we report the three-dimensional structure of CCMΔ5 bound to the peptide derived from skeletal muscle myosin light-chain kinase (skMLCK). The structure determination was achieved using multidimensional nuclear magnetic resonance (NMR) spectroscopy. The complex structure of CCM∆5-skMLCK was compared to that of wild CaM-skMLCK. The results showed that the orientation of helix-1 and helix-5 in CCM∆5 differs from those in wild CaM. Moreover, distinctive hydrophobic interaction manner was found in the binding between CCM∆5 and peptide; Phe141, Ala128, Met109, Leu105 and Phe92 of CCM∆5 contribute to the interaction with Trp4 of the skMLCK peptide.   Abbreviations: CaM, calmodulin; CCMΔX, a deletion mutant of CaM that lacks X C-terminal residues; NMR, Nuclear magnetic resonance; PDB, Protein date bank; skMLCK, skeletal muscle myosin light-chain kinase; TOF-MS, Time-of-flight mass spectrometry; RMSD, root mean square deviation; SDS-PAGE, Sodium dodecyl sulfate polyacrylamide gel electrophoresis Citation: Vu Van Dung, Umetsu Y., Ohki S., 2017. Three-dimensional structure of the complex between calmodulin mutant lacking the c-terminal five residues and the calmodulin-binding peptide derived from skeletal muscle myosin light-chain kinase. Tap chi Sinh hoc, 39(3): 309-319. DOI: 10.15625/0866-7160/v39n3.10111. *Corresponding author: [email protected] Received 19 June 2017, accepted 20 August 2017 

Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase

Biochemistry ◽  
1986 ◽  
Vol 25 (6) ◽  
pp. 1458-1464 ◽  
Author(s):  
Thomas J. Lukas ◽  
Wilson H. Burgess ◽  
Franklyn G. Prendergast ◽  
Wai Lau ◽  
D. Martin Watterson
Keyword(s):  
Binding Site ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Calmodulin Binding ◽  
Binding Domains

Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin [Erratum to document cited in CA115(19):201952d]

Biochemistry ◽  
1992 ◽  
Vol 31 (1) ◽  
pp. 316-316
Author(s):  
Sharon M. Roth ◽  
Diane M. Schneider ◽  
Laura A. Strobel ◽  
Mark F. A. VanBerkum ◽  
Anthony R. Means ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Smooth Muscle Myosin ◽  
Binding Domain ◽  
Calmodulin Binding ◽  
Domain Peptide ◽  
Muscle Myosin
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