Related ArticlesThe ATP/metallothionein interaction: NMR and STM.
Biochemistry. 2002 Feb 5;41(5):1689-94
Authors: Maret W, Heffron G, Hill HA, Djuricic D, Jiang LJ, Vallee BL
We have previously established that ATP binds to mammalian metallothionein-2 (MT). The interaction between ATP and MT and the associated conformational change of the protein affect the sulfhydryl reactivity and zinc transfer potential of MT [Jiang, L.-J., Maret, W., and Vallee, B. L. (1998) The ATP-metallothionein complex. Proc. Natl. Acad. Sci. U.S.A. 95, 9146-9149]. NMR spectroscopic investigations have now provided further evidence for the interaction. (35)Cl NMR spectroscopy has further identified chloride as an additional biological MT ligand, which can interfere with the interaction of ATP with MT. (1)H NMR/TOCSY spectra demonstrate that ATP binding affects the N- and C-terminal amino acids of the MT molecule. Scanning tunneling microscopy recorded images of single MT molecules in buffered solutions. Moreover, this technique demonstrates that the otherwise nearly linear MT molecule bends by about 20 degrees at its central hinge region between the domains in the presence of ATP. These results may bear on the development of mild obesity in MT null mice and the role of MT in the regulation of energy balance. The interaction suggests a mechanism for the cellular translocation, retention, and reactivity of the ATP*MT complex in the mitochondrial intermembrane space. Both MT and ATP are localized there, and MT and thionein alternately bind and release zinc, thereby affecting mitochondrial respiration.
[Question from NMRWiki Q&A forum] peptide protein interaction
peptide protein interaction
I have determined the structure of a 110 residues protein(11kDa) which is known to interact with a 15mer peptide. Now I am interested to know which residues of the 15mer peptide interacts with this 11kDa protein. Can anyone suggest a simple nmr experiment which can tell the residues from the 15mer peptide which interact with the protein.
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nmrlearner
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02-01-2011 06:40 PM
[CNS Yahoo group] Re: igroup interaction
Re: igroup interaction
Hi, Just a simple question: what does the map tell you about this Tyr and its symmetry related mate ? Does it really look as if they're close to within a
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nmrlearner
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12-10-2010 11:02 PM
[CNS Yahoo group] igroup interaction
igroup interaction
Hello cns users: Hoping for some insight - I have a single clash in my structure - a tyrosine side chain clashes with its symmetry self. In order to handle
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nmrlearner
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12-10-2010 11:02 PM
(13)C/(15)N-(19)F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with T
(13)C/(15)N-(19)F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with Tat Peptides.
(13)C/(15)N-(19)F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with Tat Peptides.
J Am Chem Soc. 2010 Nov 24;
Authors: Huang W, Varani G, Drobny GP
The complex of the HIV TAR RNA with the viral regulatory protein Tat is of considerable interest, but the plasticity of this interaction has made it impossible so far to establish the structure of that complex. In order to explore a new approach to obtain structural information on...
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11-26-2010 05:32 PM
13C/15N-19F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with Tat Pep
13C/15N-19F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with Tat Peptides
Wei Huang, Gabriele Varani and Gary P. Drobny
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1051439/aop/images/medium/ja-2010-051439_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1051439
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/bKQhcXWaqW0
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11-25-2010 07:22 AM
[NMR paper] 111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein
111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein.
Biochemistry. 1996 Nov 5;35(44):13929-36
Authors: Li H, Otvos JD
Metal displacement reactions of Cd7MT with Ag+ or Cu+ and interprotein metal exchange reactions between Cd7MT and Ag12MT or Cu12MT were studied by 111Cd NMR. Titration of 111Cd7MT with Ag+ indicates that...
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08-22-2010 02:20 PM
[NMR paper] Mutation of invariant cysteines of mammalian metallothionein alters metal binding cap
Mutation of invariant cysteines of mammalian metallothionein alters metal binding capacity, cadmium resistance, and 113Cd NMR spectrum.
Related Articles Mutation of invariant cysteines of mammalian metallothionein alters metal binding capacity, cadmium resistance, and 113Cd NMR spectrum.
J Biol Chem. 1991 Dec 25;266(36):24390-7
Authors: Cismowski MJ, Narula SS, Armitage IM, Chernaik ML, Huang PC
Using a yeast expression vector system, we have expressed both wild type and six mutated Chinese hamster metallothionein coding sequences in a...
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08-21-2010 11:12 PM
[NMR paper] Mutation of invariant cysteines of mammalian metallothionein alters metal binding cap
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Related Articles Mutation of invariant cysteines of mammalian metallothionein alters metal binding capacity, cadmium resistance, and 113Cd NMR spectrum.
J Biol Chem. 1991 Dec 25;266(36):24390-7
Authors: Cismowski MJ, Narula SS, Armitage IM, Chernaik ML, Huang PC
Using a yeast expression vector system, we have expressed both wild type and six mutated Chinese hamster metallothionein coding sequences in a...
The ATP/metallothionein interaction: NMR and STM.
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