Related ArticlesA selective NMR probe to monitor the conformational transition from inactive to active kinase.
ACS Chem Biol. 2014 Sep 23;
Authors: Xie Q, Fulton DB, Andreotti AH
Abstract
Kinases control many aspects of cellular signaling and are therefore therapeutic targets for numerous disease states. Monitoring the conformational changes that drive activation and inactivation of the catalytic kinase core is a challenging experimental problem due to the dynamic nature of these enzymes. We apply [13C] reductive methylation to chemically introduce NMR active nuclei into unlabeled protein kinases. The results demonstrate that solution NMR spectroscopy can be used to monitor specific changes in the chemical environment of structurally important lysines in a [13C] methylated kinase as it shifts from the inactive to active state. This approach provides a solution based method to complement x-ray crystallographic data and can be applied to nearly any kinase, regardless of size or method of production.
PMID: 25248068 [PubMed - as supplied by publisher]
[NMR paper] Solution NMR Structures of Active Pyrenophora tritici-repentis ToxB and its Inactive Homolog Reveal Potential Determinants of Toxin Activity.
Solution NMR Structures of Active Pyrenophora tritici-repentis ToxB and its Inactive Homolog Reveal Potential Determinants of Toxin Activity.
Related Articles Solution NMR Structures of Active Pyrenophora tritici-repentis ToxB and its Inactive Homolog Reveal Potential Determinants of Toxin Activity.
J Biol Chem. 2014 Jul 26;
Authors: Nyarko A, Singarapu KK, Figueroa M, Manning VA, Pandelova I, Wolpert TJ, Ciuffetti LM, Barbar E
Abstract
Ptr ToxB (ToxB) is a proteinaceous host-selective toxin produced by Pyrenophora...
nmrlearner
Journal club
0
07-30-2014 10:22 AM
[NMR paper] A Conformational Ensemble Derived Using NMR Methyl Chemical Shifts Reveals a Mechanical Clamping Transition That Gates the Binding of the HU Protein to DNA.
A Conformational Ensemble Derived Using NMR Methyl Chemical Shifts Reveals a Mechanical Clamping Transition That Gates the Binding of the HU Protein to DNA.
Related Articles A Conformational Ensemble Derived Using NMR Methyl Chemical Shifts Reveals a Mechanical Clamping Transition That Gates the Binding of the HU Protein to DNA.
J Am Chem Soc. 2014 Feb 12;136(6):2204-7
Authors: Kannan A, Camilloni C, Sahakyan AB, Cavalli A, Vendruscolo M
Abstract
Recent improvements in the accuracy of structure-based methods for the prediction of...
nmrlearner
Journal club
0
02-13-2014 03:35 PM
[NMR paper] The synthesis, characterization, and application of (13)c-methyl isocyanide as an NMR probe of heme protein active sites.
The synthesis, characterization, and application of (13)c-methyl isocyanide as an NMR probe of heme protein active sites.
Related Articles The synthesis, characterization, and application of (13)c-methyl isocyanide as an NMR probe of heme protein active sites.
Methods Mol Biol. 2013;987:51-9
Authors: McCullough C, Pullela PK, Im SC, Waskell L, Sem D
Abstract
The cytochromes P450 (CYPs) play a central role in a variety of important biological oxidations, such as steroid synthesis and the metabolism of xenobiotic compounds, including most...
nmrlearner
Journal club
0
03-12-2013 07:09 PM
Conformational Study of 9-Dehydro-9-Trifluoromethyl Cinchona Alkaloids via 19F NMR Spectroscopy: Emergence of Trifluoromethyl Moiety as a Conformational Stabilizer and a Probe
Conformational Study of 9-Dehydro-9-Trifluoromethyl Cinchona Alkaloids via 19F NMR Spectroscopy: Emergence of Trifluoromethyl Moiety as a Conformational Stabilizer and a Probe
G. K. Surya Prakash, Fang Wang, Chuanfa Ni, Jingguo Shen, Ralf Haiges, Andrei K. Yudin, Thomas Mathew and George A. Olah
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202373d/aop/images/medium/ja-2011-02373d_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202373d
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
nmrlearner
Journal club
0
06-14-2011 02:30 AM
[NMR paper] NMR investigation of the alkaline-like conformational transition of horse heart cytoc
NMR investigation of the alkaline-like conformational transition of horse heart cytochrome c in the presence of exogenous thiazole.
Related Articles NMR investigation of the alkaline-like conformational transition of horse heart cytochrome c in the presence of exogenous thiazole.
Biophys Chem. 2003 Jun 1;104(2):459-68
Authors: Yao Y, Tang W
The conformational transition of horse heart cyt c in the presence of exogenous thiazole is investigated by NMR spectroscopy. Surprisingly, besides the native form and the ligand-bound form, another species...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] Analysis of stress in the active site of myosin accompanied by conformational changes
Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy.
Related Articles Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy.
Eur J Biochem. 1998 Mar 15;252(3):520-9
Authors: Maruta S, Henry GD, Ohki T, Kambara T, Sykes BD, Ikebe M
Myosin forms stable ternary complexes with ADP and the...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of
Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR.
J Mol Biol. 1994 Jan 7;235(1):287-301
Authors: Morellet N, de Rocquigny H, Mély Y, Jullian N, Déméné H, Ottmann M, Gérard D, Darlix JL, Fournie-Zaluski MC, Roques BP
The nucleocapsid protein NCp7 of...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of
Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR.
J Mol Biol. 1994 Jan 7;235(1):287-301
Authors: Morellet N, de Rocquigny H, Mély Y, Jullian N, Déméné H, Ottmann M, Gérard D, Darlix JL, Fournie-Zaluski MC, Roques BP
The nucleocapsid protein NCp7 of...
A selective NMR probe to monitor the conformational transition from inactive to active kinase.
Linear Mode
