Related ArticlesMapping the interacting regions between troponins T and C. Binding of TnT and TnI peptides to TnC and NMR mapping of the TnT-binding site on TnC.
Muscular contraction is triggered by an increase in calcium concentration, which is transmitted to the contractile proteins by the troponin complex. The interactions among the components of the troponin complex (troponins T, C, and I) are essential to understanding the regulation of muscle contraction. While the structure of TnC is well known, and a model for the binary TnC.TnI complex has been recently published (Tung, C.-S., Wall, M. E., Gallagher, S. C., and Trewhella, J. (2000) Protein Sci. 9, 1312-1326), very little is known about TnT. Using non-denaturing gels and NMR spectroscopy, we have analyzed the interactions between TnC and five peptides from TnT as well as how three TnI peptides affect these interactions. Rabbit fast skeletal muscle peptide TnT-(160-193) binds to TnC with a dissociation constant of 30 +/- 6 microm. This binding still occurs in the presence of TnI-(1-40) but is prevented by the presence of TnI-(56-115) or TnI-(96-139), both containing the primary inhibitory region of TnI. TnT-(228-260) also binds TnC. The binding site for TnT-(160-193) is located on the C-terminal domain of TnC and was mapped to the surface of TnC using NMR chemical shift mapping techniques. In the context of the model for the TnC.TnI complex, we discuss the interactions between TnT and the other troponin subunits.
[NMR paper] NMR dynamics-derived insights into the binding properties of a peptide interacting wi
NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain.
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Biochemistry. 2005 Jan 18;44(2):694-703
Authors: Finerty PJ, Mittermaier AK, Muhandiram R, Kay LE, Forman-Kay JD
The signal transduction protein phospholipase C-gamma1 (PLC-gamma1) is activated when its C-terminal SH2 domain (PLCC) binds the phosphorylated Tyr-1021 site (pTyr-1021) in the beta-platelet-derived growth factor...
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[NMR paper] Calbindin D28K interacts with Ran-binding protein M: identification of interacting do
Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
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Biochem Biophys Res Commun. 2003 Apr 18;303(4):1186-92
Authors: Lutz W, Frank EM, Craig TA, Thompson R, Venters RA, Kojetin D, Cavanagh J, Kumar R
Calbindin D(28K) is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D(28K) interacts...
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[NMR paper] Mapping the cytochrome c553 interacting site using 1H and 15N NMR.
Mapping the cytochrome c553 interacting site using 1H and 15N NMR.
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FEBS Lett. 1999 Oct 22;460(1):77-80
Authors: Morelli X, Guerlesquin F
Cytochrome c553 is the electron transfer partner of formate dehydrogenase and of
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Evaluation of protein adsorption and preferred binding regions in multimodal chromato
Evaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR
Chung, W. K., Freed, A. S., Holstein, M. A., McCallum, S. A., Cramer, S. M....
Date: 2010-09-28
NMR titration experiments with labeled human ubiquitin were employed in concert with chromatographic data obtained with a library of ubiquitin mutants to study the nature of protein adsorption in multimodal (MM) chromatography. The elution order of the mutants on the MM resin was significantly different from that obtained by ion-exchange chromatography. Further, the chromatographic results...
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Evaluation of protein adsorption and preferred binding regions in multimodal chromato
Evaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR.
Related Articles Evaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR.
Proc Natl Acad Sci U S A. 2010 Sep 13;
Authors: Chung WK, Freed AS, Holstein MA, McCallum SA, Cramer SM
NMR titration experiments with labeled human ubiquitin were employed in concert with chromatographic data obtained with a library of ubiquitin mutants to study the nature of protein adsorption in multimodal (MM) chromatography....
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[NMR paper] NMR evidence for similarities between the DNA-binding regions of Drosophila melanogas
NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Related Articles NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Biochemistry. 1994 Jan 11;33(1):10-6
Authors: Vuister GW, Kim SJ, Wu C, Bax A
Heteronuclear multidimensional NMR experiments of residues 33-163 of the...
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[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
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J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...
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[NMR paper] NMR evidence for similarities between the DNA-binding regions of Drosophila melanogas
NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Related Articles NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Biochemistry. 1994 Jan 11;33(1):10-6
Authors: Vuister GW, Kim SJ, Wu C, Bax A
Heteronuclear multidimensional NMR experiments of residues 33-163 of the...
Mapping the interacting regions between troponins T and C. Binding of TnT and TnI pep
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