Related ArticlesA model of reversible inhibitors in the gastric H+/K+-ATPase binding site determined by rotational echo double resonance NMR.
J Biol Chem. 2001 Nov 16;276(46):43197-204
Authors: Watts JA, Watts A, Middleton DA
Several close analogues of the noncovalent H(+)/K(+)-ATPase inhibitor SCH28080 (2-methyl-3-cyanomethyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine) have been screened for activity and examined in the pharmacological site of action by solid-state NMR spectroscopy. TMPIP, the 1,2,3-trimethyl analogue of SCH28080, and variants of TMPIP containing fluorine in the phenylmethoxy ring exhibited IC(50) values for porcine H(+)/K(+)-ATPase inhibition falling in the sub-10 microm range. Deuterium NMR spectra of a (2)H-labeled inhibitor titrated into H(+)/K(+)-ATPase membranes revealed that 80-100% of inhibitor was bound to the protein, and K(+)-competition (2)H NMR experiments confirmed that the inhibitor lay within the active site. The active binding conformation of the pentafluorophenylmethoxy analogue of TMPIP was determined from (13)C-(19)F dipolar coupling measurements using the cross-polarization magic angle spinning NMR method, REDOR. It was found that the inhibitor adopts an energetically favorable extended conformation falling between fully planar and partially bowed extremes. These findings allowed a model to be proposed for the binding of this inhibitor to H(+)/K(+)-ATPase based on the results of independent site-directed mutagenesis studies. In the model, the partially bowed inhibitor interacts with Phe(126) close to the N-terminal membrane spanning helix M1 and residues in the extracellular loop bridging membrane helices M5 and M6 and is flanked by residues in M4.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Biochem Biophys Res Commun. 2010 Dec 24;
Authors: Myint W, Gong Q, Ahn J, Ishima R
Sarcoplasmic reticulum Ca(2+) ATPase (SERCA) is essential for muscle function by transporting Ca(2+) from the cytosol into the sarcoplasmic reticulum through ATP hydrolysis. In this report, the effects of substitution mutations on the...
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[NMR paper] Location of the Zn(2+)-binding site on S100B as determined by NMR spectroscopy and si
Location of the Zn(2+)-binding site on S100B as determined by NMR spectroscopy and site-directed mutagenesis.
Related Articles Location of the Zn(2+)-binding site on S100B as determined by NMR spectroscopy and site-directed mutagenesis.
Biochemistry. 2003 Nov 25;42(46):13410-21
Authors: Wilder PT, Baldisseri DM, Udan R, Vallely KM, Weber DJ
In addition to binding Ca(2+), the S100 protein S100B binds Zn(2+) with relatively high affinity as confirmed using isothermal titration calorimetry (ITC; K(d) = 94 +/- 17 nM). The Zn(2+)-binding site on...
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[NMR paper] In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5
In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction.
Related Articles In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction.
J Med Chem. 2002 Dec 19;45(26):5655-60
Authors: Kamionka M, Rehm T, Beisel HG, Lang K, Engh RA, Holak TA
Recently we have determined the crystal structure of the insulin-like growth factor-I (IGF-I) in complex with the N-terminal domain of the IGF-binding protein-5 (IGFBP-5). Here we report results of computer screening for...
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[NMR paper] NMR-based discovery of lead inhibitors that block DNA binding of the human papillomav
NMR-based discovery of lead inhibitors that block DNA binding of the human papillomavirus E2 protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR-based discovery of lead inhibitors that block DNA binding of the human papillomavirus E2 protein.
J Med Chem. 1997 Sep 26;40(20):3144-50
Authors: Hajduk PJ, Dinges J, Miknis GF, Merlock M, Middleton T, Kempf DJ, Egan DA, Walter KA, Robins TS, Shuker SB, Holzman TF, Fesik SW
The E2 protein is required for the replication of human...
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[NMR paper] A model of the iron responsive element RNA hairpin loop structure determined from NMR
A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data.
Biochemistry. 1996 Oct 22;35(42):13586-96
Authors: Laing LG, Hall KB
The iron responsive element (IRE) is a conserved RNA structure that is found in the 5' UTR of ferritin mRNA and in the 3' UTR of transferrin receptor mRNA....
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[NMR paper] Temperature-reversible eruptions of vesicles in model membranes studied by NMR.
Temperature-reversible eruptions of vesicles in model membranes studied by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Temperature-reversible eruptions of vesicles in model membranes studied by NMR.
Biophys J. 1992 May;61(5):1413-26
Authors: Nezil FA, Bayerl S, Bloom M
Deuterium (2H) and phosphorus (31P) nuclear magnetic resonance (NMR) and...
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08-21-2010 11:41 PM
[NMR paper] Structure of human cyclophilin and its binding site for cyclosporin A determined by X
Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.
Nature. 1991 Sep 19;353(6341):276-9
Authors: Kallen J, Spitzfaden C, Zurini MG, Wider G, Widmer H, Wüthrich K, Walkinshaw MD
The protein cyclophilin is the major intracellular...
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[NMR paper] Structure of human cyclophilin and its binding site for cyclosporin A determined by X
Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.
Nature. 1991 Sep 19;353(6341):276-9
Authors: Kallen J, Spitzfaden C, Zurini MG, Wider G, Widmer H, Wüthrich K, Walkinshaw MD
The protein cyclophilin is the major intracellular...