NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII
NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII
Abstract
Messenger RNA is recruited to the eukaryotic ribosome by a complex including the eukaryotic initiation factor (eIF) 4E (the cap-binding protein), the scaffold protein eIF4G and the RNA helicase eIF4A. To shut off host-cell protein synthesis, eIF4G is cleaved during picornaviral infection by a virally encoded proteinase; the structural basis of this reaction and its stimulation by eIF4E is unclear. We have structurally and biochemically investigated the...
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NMR Structure and Dynamics of the C-Terminal Domain from Human Rev1 and Its Complex with Rev1 Interacting Region of DNA Polymerase ?
NMR Structure and Dynamics of the C-Terminal Domain from Human Rev1 and Its Complex with Rev1 Interacting Region of DNA Polymerase ?
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Biochemistry
DOI: 10.1021/bi300566z
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[NMR paper] Conformational differences between complexes of elongation factor Tu studied 19F-NMR
Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
Eur J Biochem. 1993 Dec 15;218(3):1041-7
Authors: Eccleston JF, Molloy DP, Hinds MG, King RW, Feeney J
An analogue of elongation factor Tu (EF-Tu) from Escherichia coli was prepared by...
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08-22-2010 03:01 AM
[NMR paper] Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophil
Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR.
Related Articles Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR.
Biochemistry. 1992 Mar 24;31(11):2970-7
Authors: Limmer S, Reiser CO, Schirmer NK, Grillenbeck NW, Sprinzl M
Proton NMR experiments of the GTP/GDP-binding protein EF-Tu from the extremely thermophilic bacterium Thermus thermophilus HB8 in H2O have been performed paying special attention to the...
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[NMR paper] The carboxyl-terminal region of human interferon gamma is important for biological ac
The carboxyl-terminal region of human interferon gamma is important for biological activity: mutagenic and NMR analysis.
Related Articles The carboxyl-terminal region of human interferon gamma is important for biological activity: mutagenic and NMR analysis.
Protein Eng. 1991 Feb;4(3):335-41
Authors: Lundell D, Lunn C, Dalgarno D, Fossetta J, Greenberg R, Reim R, Grace M, Narula S
Deletion of nine amino acids from the carboxyl terminus of human IFN gamma (residues 138--146; LFRGRRASQ) resulted in a 7-fold increase in specific antiviral...
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[NMR paper] Examination of elongation factor Tu for aluminum fluoride binding sites using fluores
Examination of elongation factor Tu for aluminum fluoride binding sites using fluorescence and 19F-NMR methodologies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Examination of elongation factor Tu for aluminum fluoride binding sites using fluorescence and 19F-NMR methodologies.
FEBS Lett. 1991 Jan 28;278(2):225-8
Authors: Hazlett TL, Higashijima T, Jameson DM
This article reports on a comparison of the interaction of Al3+ and F- with two GTP-binding proteins,...
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[NMR paper] NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu
NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Related Articles NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Biochemistry. 1991 Nov 12;30(45):10872-7
Authors: Lowry DF, Cool RH, Redfield AG, Parmeggiani A
The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide...
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[NMR paper] NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu
NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Related Articles NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Biochemistry. 1991 Nov 12;30(45):10872-7
Authors: Lowry DF, Cool RH, Redfield AG, Parmeggiani A
The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide...