Related ArticlesCalbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
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 with Ran-binding protein M, a protein known to play a role in microtubule function. Using NMR methods, we show that a peptide, LASIKNR, derived from Ran-binding protein M, interacts with several regions of the calcium-loaded protein including the amino terminus and two other regions that exhibit conformational exchange on the NMR timescale. We suggest that the interaction between calbindin D(28K) and Ran-binding protein M may be important in calbindin D(28K) function.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Methods Enzymol. 2011;493:241-75
Authors: Ziarek JJ, Peterson FC, Lytle BL, Volkman BF
Over the last 15years, the role of NMR spectroscopy in the lead identification and optimization stages of pharmaceutical drug discovery has steadily increased. NMR occupies a unique niche in the biophysical analysis of drug-like...
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Solution structure of the human Tax-interacting protein-1
Solution structure of the human Tax-interacting protein-1
Solution structure of the human Tax-interacting protein-1
Content Type Journal Article
Pages 329-334
DOI 10.1007/s10858-009-9361-8
Authors
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01-09-2011 12:46 PM
[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.
Related Articles NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain.
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] 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] Mapping the interacting regions between troponins T and C. Binding of TnT and TnI pep
Mapping 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.
Related Articles Mapping 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.
J Biol Chem. 2001 Sep 28;276(39):36606-12
Authors: Blumenschein TM, Tripet BP, Hodges RS, Sykes BD
Muscular contraction is triggered by an increase in calcium concentration, which is transmitted to the contractile proteins by the troponin...
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11-19-2010 08:44 PM
[NMR paper] Identification of the bile acid-binding site of the ileal lipid-binding protein by ph
Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
Related Articles Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
J Biol Chem. 2001 Mar 9;276(10):7291-301
Authors: Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C
...
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[NMR paper] Identification of the DNA binding surface of H-NS protein from Escherichia coli by he
Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
Related Articles Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
FEBS Lett. 1999 Jul 16;455(1-2):63-9
Authors: Shindo H, Ohnuki A, Ginba H, Katoh E, Ueguchi C, Mizuno T, Yamazaki T
The DNA binding domain of H-NS protein was studied with various N-terminal deletion mutant proteins and identified by gel retardation assay and heteronuclear 2D- and 3D-NMR...
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11-18-2010 08:31 PM
[NMR paper] Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid
Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy.
Related Articles Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy.
Biochemistry. 1990 Apr 24;29(16):3828-34
Authors: Van Gorkom LC, Horváth LI, Hemminga MA, Sternberg B, Watts A
The major coat protein of M13 bacteriophage has been incorporated into bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine, deuterated in the trimethyl segments of...