Related ArticlesInteraction of calmodulin with phospholamban and caldesmon: comparative studies by 1H-NMR spectroscopy.
Biochim Biophys Acta. 1992 Nov 10;1160(1):22-34
Authors: Gao Y, Levine BA, Mornet D, Slatter DA, Strasburg GM
In order to identify comparative aspects of the interaction of calmodulin with its target proteins, proton magnetic-resonance studies of complex formation between calmodulin and defined segments of phospholamban and caldesmon have been undertaken. Residues 3-15 in the cytoplasmic region of phospholamban, an integral membrane protein of cardiac sarcoplasmic reticulum believed to regulate the calcium pumping ATPase, are shown to contribute to interaction with calmodulin. Using wheat germ calmodulin specifically modified with a spin-label to provide the spectral means for spatial localisation, these residues of phospholamban were correlated with binding in the vicinity of the probe attached to Cys-27 in the N-terminal domain of calmodulin. This interaction, relevant to the mechanism of calmodulin-dependent phosphorylation of phospholamban that relieves its inhibitory influence on the calcium pump, provides a useful model system for comparative study of the properties of calmodulin-binding domains. We contrast here a calmodulin-binding segment in the C-terminal region of caldesmon localised by 1H-NMR study of the interface(s) between the two proteins. These observations are discussed in the context of other calmodulin-binding sequences.
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] Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Related Articles Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Mol Membr Biol. 2005 Jul-Aug;22(4):353-61
Authors: Hughes E, Middleton DA
Phospholamban (PLB) is a small transmembrane protein that regulates calcium transport across the sarcoplasmic reticulum (SR) of cardiac cells via a reversible inhibitory interaction with Ca2+-ATPase. In this work...
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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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Comparative NMR studies demonstrate profound differences between two viroporins: P7 o
Comparative NMR studies demonstrate profound differences between two viroporins: P7 of HCV and Vpu of HIV-1.
Related Articles Comparative NMR studies demonstrate profound differences between two viroporins: P7 of HCV and Vpu of HIV-1.
Biochim Biophys Acta. 2010 Aug 18;
Authors: Cook GA, Zhang H, Park SH, Wang Y, Opella SJ
The p7 protein from hepatitis C virus and the Vpu protein from HIV-1 are members of the viroporin family of small viral membrane proteins. It is essential to determine their structures in order to obtain an understanding of their...
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08-25-2010 02:04 PM
[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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08-22-2010 03:31 PM
[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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08-22-2010 03:03 PM
[NMR paper] Comparative studies of the interaction of human and bovine platelet factor 4 with hep
Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes.
Related Articles Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes.
J Protein Chem. 1993 Jun;12(3):303-9
Authors: Talpas CJ, Lee L
The pKa values of His-38 and His-50 of the heparin-binding protein, bovine platelet factor 4, are 5.6 and 6.5, respectively, as determined by 1H NMR spectroscopy. The 1H NMR...
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[NMR paper] Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calci
Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II.
Related Articles Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II.
Biochemistry. 1991 Oct 22;30(42):10236-45
Authors: Brito RM, Putkey JA, Strynadka NC, James MN, Rosevear PR
One- and two-dimensional NMR techniques were used to study both the influence of mutations on the structure of recombinant normal cardiac troponin C (cTnC3) and the conformational changes induced by Ca2+ binding to site II,...
Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H
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