Related ArticlesMelatonin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemical studies.
Biochim Biophys Acta. 1998 Mar 3;1383(1):37-47
Authors: Ouyang H, Vogel HJ
It has been reported that the hormone melatonin binds tightly to the ubiquitous calcium-regulatory protein, calmodulin (CaM) with a Kd value around 0.1 nM [Benítez-King et al., Biochim. Biophys. Acta, 1290 (1993) 191-196]. Normally CaM only binds to target proteins and various 20-residue synthetic peptides encompassing the CaM-binding domain of these target proteins with K(d) values ranging between 1.0 microM and 0.1 nM. Here we have studied the interaction of melatonin and several structurally related compounds--serotonin, 5-hydroxytryptophan, and tryptophan--to CaM through gel band shift assays, enzymatic competition assays with calcineurin, fluorescence spectroscopy, far and near UV circular dichroism spectropolarimetry and NMR spectroscopy. Fluorescence spectra show that the binding is calcium dependent. NMR studies with biosynthetically labelled methyl-13C-Met CaM show that melatonin and the other compounds interact with the hydrophobic cleft regions of the protein. Our NMR data show that melatonin binds to both domains of the dumbbell-shaped CaM, while serotonin appears to bind only to the C-terminal domain. This binding mode is further substantiated by fluorescence and gel band shift competition experiments with synthetic peptides from myosin light chain kinase and constitutive nitric oxide synthase. Circular dichroism spectra indicate that the secondary structure of CaM is not altered by addition of melatonin. Our data are internally consistent and reveal Kd values in the mM range for melatonin. Thus the binding of these compounds to CaM is substantially weaker than was previously reported and is unlikely to be of physiological significance.
NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin.
NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin.
NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin.
Biochim Biophys Acta. 2011 May 24;
Authors: Chen AS, Kim YM, Gayen S, Huang Q, Raida M, Kang C
The serotonin (5-HT(1A)) receptor, a G-protein-coupled receptor (GPCR), plays important roles in serotonergic signaling in the central nervous system. The third intracellular loop (ICL3) of the 5-HT(1A) receptor has...
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[NMR paper] NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
Related Articles NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
Protein Sci. 2004 Nov;13(11):2925-38
Authors: Turjanski AG, Estrin DA, Rosenstein RE, McCormick JE, Martin SR, Pastore A, Biekofsky RR, Martorana V
Pineal hormone melatonin (N-acetyl-5-methoxytryptamine) is thought to modulate the calcium/calmodulin signaling pathway either by changing intracellular Ca(2+) concentration via activation of its G-protein-coupled...
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[NMR paper] NMR studies of caldesmon-calmodulin interactions.
NMR studies of caldesmon-calmodulin interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of caldesmon-calmodulin interactions.
Biochemistry. 1997 Mar 11;36(10):2817-25
Authors: Zhou N, Yuan T, Mak AS, Vogel HJ
The binding of the calcium-regulatory protein calmodulin (CaM) to caldesmon (CaD) contributes to the regulation of smooth muscle contraction. Two regions of caldesmon have been identified as putative calmodulin-binding domains. We have earlier reported on the...
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[NMR paper] NMR studies of caldesmon-calmodulin interactions.
NMR studies of caldesmon-calmodulin interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of caldesmon-calmodulin interactions.
Biochemistry. 1997 Mar 11;36(10):2817-25
Authors: Zhou N, Yuan T, Mak AS, Vogel HJ
The binding of the calcium-regulatory protein calmodulin (CaM) to caldesmon (CaD) contributes to the regulation of smooth muscle contraction. Two regions of caldesmon have been identified as putative calmodulin-binding domains. We have earlier reported on the...
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[NMR paper] Protein engineering and NMR studies of calmodulin.
Protein engineering and NMR studies of calmodulin.
Related Articles Protein engineering and NMR studies of calmodulin.
Mol Cell Biochem. 1995 Aug-Sep;149-150:3-15
Authors: Vogel HJ, Zhang M
The calcium regulatory protein calmodulin (CaM) plays a role as an on-off switch in the activation of many enzymes and proteins. CaM has a dumbbell shaped structure with two folded domains, which are connected by a flexible linker in solution. The calmodulin-binding domains of the target proteins are contained in 20 residue long amino acid sequences, that...
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[NMR paper] Two-dimensional NMR studies of selenomethionyl calmodulin.
Two-dimensional NMR studies of selenomethionyl calmodulin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Two-dimensional NMR studies of selenomethionyl calmodulin.
J Mol Biol. 1994 Jun 17;239(4):545-54
Authors: Zhang M, Vogel HJ
Calmodulin (CaM) is a ubiquitous calcium regulatory protein that can interact with almost 30 different target proteins. The majority of the CaM-binding domains of the target proteins are believed to interact with two hydrophobic surfaces on...
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[NMR paper] Characterization of trimethyllysine 115 in calmodulin by 14N and 13C NMR spectroscopy
Characterization of trimethyllysine 115 in calmodulin by 14N and 13C NMR spectroscopy.
Related Articles Characterization of trimethyllysine 115 in calmodulin by 14N and 13C NMR spectroscopy.
J Biol Chem. 1994 Feb 18;269(7):5099-105
Authors: Zhang M, Huque E, Vogel HJ
In this paper, we describe three approaches to study the single trimethyllysine 115 in calmodulin. First, 14N NMR spectroscopy has been used as a novel spectroscopic tool. Because of the unique symmetrical tetrahedral substitution of its side chain, the trimethyllysine residue...
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[NMR paper] 1H NMR spectroscopic studies on the interactions between human plasma antithrombin II
1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.
Related Articles 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.
Biochemistry. 1992 Mar 3;31(8):2286-94
Authors: Horne A, Gettins P
The effects of length and composition upon the antithrombin-binding properties of heparin have been investigated for two series of structurally related heparin oligosaccharides. Each...
Melatonin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemi
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