Related ArticlesTriple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Biochemistry. 1991 Jun 4;30(22):5498-504
Authors: Ikura M, Kay LE, Krinks M, Bax A
Heteronuclear 3D and 4D NMR experiments have been used to obtain 1H, 13C, and 15N backbone chemical shift assignments in Ca(2+)-loaded calmodulin complexed with a 26-residue synthetic peptide (M13) corresponding to the calmodulin-binding domain (residues 577-602) of rabbit skeletal muscle myosin light-chain kinase. Comparison of the chemical shift values with those observed in peptide-free calmodulin [Ikura, M., Kay, L. E., & Bax, A. (1990) Biochemistry 29, 4659-4667] shows that binding of M13 peptide induces substantial chemical shift changes that are not localized in one particular region of the protein. The largest changes are found in the first helix of the Ca(2+)-binding site I (E11-E14), the N-terminal portion of the central helix (M72-D78), and the second helix of the Ca(2+)-binding site IV (F141-M145). Analysis of backbone NOE connectivities indicates a change from alpha-helical to an extended conformation for residues 75-77 upon complexation with M13. This conformational change is supported by upfield changes in the C alpha and carbonyl chemical shifts of these residues relative to M13-free calmodulin and by hydrogen-exchange experiments that indicate that the amide protons of residues 75-82 are in fast exchange (kexch greater than 10 s-1 at pH 7, 35 degrees C) with the solvent. No changes in secondary structure are observed for the first helix of site I or the C-terminal helix of site IV. Upon complexation with M13, a significant decrease in the amide exchange rate is observed for residues T110, L112, G113, and E114 at the end of the second helix of site III.
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] Metal ion binding to calmodulin: NMR and fluorescence studies.
Metal ion binding to calmodulin: NMR and fluorescence studies.
Related Articles Metal ion binding to calmodulin: NMR and fluorescence studies.
Biometals. 1998 Sep;11(3):213-22
Authors: Ouyang H, Vogel HJ
Calmodulin is an important second messenger protein which is involved in a large variety of cellular pathways. Calmodulin is sensitive to fluctuations in the intracellular Ca2+ levels and is activated by the binding of four Ca2+ ions. In spite of the important role it plays in signal transduction pathways, it shows a surprisingly broad...
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[NMR paper] The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of p
The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins.
Related Articles The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins.
Annu Rev Biophys Biomol Struct. 1998;27:357-406
Authors: Gardner KH, Kay LE
During the past thirty years, deuterium labeling has been used to improve the resolution and sensitivity of protein NMR spectra used in a wide variety of applications. Most recently, the combination of triple resonance experiments and 2H, 13C, 15N labeled samples has...
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[NMR paper] Strong and weak binding of water to proteins studied by NMR triple-quantum filtered r
Strong and weak binding of water to proteins studied by NMR triple-quantum filtered relaxation spectroscopy of (17)O-water.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Strong and weak binding of water to proteins studied by NMR triple-quantum filtered relaxation spectroscopy of (17)O-water.
Biophys Chem. 1997 Sep 1;67(1-3):187-98
Authors: Torres AM, Grieve SM, Chapman BE, Kuchel PW
The triple-quantum filtered (TQF) spin-echo signal of (17)O-water, in the presence...
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[NMR paper] The NMR solution structure of intestinal fatty acid-binding protein complexed with pa
The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm.
J Mol Biol. 1996 Dec 6;264(3):585-602
Authors: Hodsdon ME, Ponder JW, Cistola DP
The three-dimensional solution structure of rat...
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[NMR paper] Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of
Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.
Related Articles Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.
Toxicol Lett. 1995 Dec;82-83:577-89
Authors: Hsu VL, Jia X, Kearns DR
The solution structure of a type II DNA-binding protein (DBPII), transcription factor 1 (TF1), has been determined using NMR spectroscopy. A multidimensional, heteronuclear strategy was employed to overcome assignment ambiguities due to...
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[NMR paper] Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escheri
Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli.
Related Articles Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli.
J Biomol NMR. 1992 Mar;2(2):149-60
Authors: Tjandra N, Simplaceanu V, Cottam PF, Ho C
Specific and uniform 15N labelings along with site-directed mutagenesis of glutamine-binding protein have been utilized to obtain assignments of the His156, Trp32 and Trp220 residues. These assignments have been made not only to further study the...
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[NMR paper] Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched
Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination.
Related Articles Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination.
Ciba Found Symp. 1991;161:108-19; discussion 119-35
Authors: Bax A, Ikura M, Kay LE, Barbato G, Spera S
A procedure is described that affords complete 1H, 13C and 15N resonance assignment in proteins of up to about 25 kDa. The new...
Triple-resonance multidimensional NMR study of calmodulin complexed with the binding
Linear Mode
