Related ArticlesStructural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches.
Structure. 2004 Apr;12(4):633-44
Authors: Dominguez C, Bonvin AM, Winkler GS, van Schaik FM, Timmers HT, Boelens R
The protein CNOT4 possesses an N-terminal RING finger domain that acts as an E3 ubiquitin ligase and specifically interacts with UbcH5B, a ubiquitin-conjugating enzyme. The structure of the CNOT4 RING domain has been solved and the amino acids important for the binding to UbcH5B have been mapped. Here, the residues of UbcH5B important for the binding to CNOT4 RING domain were identified by NMR chemical shift perturbation experiments, and these data were used to generate structural models of the complex with the program HADDOCK. Together with the NMR data, additional biochemical data were included in a second docking, and comparisons of the resulting model with the structure of the c-Cbl/UbcH7 complex reveal some significant differences, notably at specific residues, and give structural insights into the E2/E3 specificity.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Proc Natl Acad Sci U S A. 2011 Jul 5;
Authors: Kato H, van Ingen H, Zhou BR, Feng H, Bustin M, Kay LE, Bai Y
Chromatin structure and function are regulated by numerous proteins through specific binding to nucleosomes. The structural basis of many of these interactions is unknown, as in the case of the high mobility...
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[NMR paper] Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
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FEBS Lett. 2005 Aug 29;579(21):4585-90
Authors: Palma PN, Lagoutte B, Krippahl L, Moura JJ, Guerlesquin F
Ferredoxin (Fd) and ferredoxin-NADP(+)-reductase (FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance...
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[NMR paper] Structural genomics and the metabolome: combining computational and NMR methods to id
Structural genomics and the metabolome: combining computational and NMR methods to identify target ligands.
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Curr Opin Drug Discov Devel. 2004 Jan;7(1):62-8
Authors: Parsons L, Orban J
One of the goals of structural genomics is to use three-dimensional structures to gain insights into the function of poorly understood or hypothetical proteins. Approximate functions are often apparent from the protein fold, but more...
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[NMR paper] Filtering and selection of structural models: combining docking and NMR.
Filtering and selection of structural models: combining docking and NMR.
Related Articles Filtering and selection of structural models: combining docking and NMR.
Proteins. 2003 Oct 1;53(1):18-32
Authors: Dobrodumov A, Gronenborn AM
It is generally accepted that protein structures are more conserved than protein sequences, and 3D structure determination by computer simulations have become an important necessity in the postgenomic area. Despite major successes no robust, fast, and automated ab initio prediction algorithms for deriving accurate...
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11-24-2010 09:16 PM
[NMR paper] Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the ap
Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the application of a sensitivity optimized isotope-filtered NOESY experiment.
Related Articles Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the application of a sensitivity optimized isotope-filtered NOESY experiment.
J Biomol NMR. 2001 Mar;19(3):231-41
Authors: Iwahara J, Wojciak JM, Clubb RT
The NMR spectra of the complex between the DNA-binding domain of the Dead ringer protein (DRI-DBD, Gly262-Gly398) and its DNA binding site...
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11-19-2010 08:32 PM
[NMR paper] The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex
The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.
Related Articles The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.
J Mol Biol. 1999 Sep 3;291(5):1067-77
Authors: Wilkinson KD, Laleli-Sahin E, Urbauer J, Larsen CN, Shih GH, Haas AL, Walsh ST, Wand AJ
The ubiquitin fold is a versatile and widely used targeting signal that is added post-translationally to a variety of proteins. Covalent attachment of one or more...
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11-18-2010 08:31 PM
[NMR paper] Structural changes caused by site-directed mutagenesis of tyrosine-98 in Desulfovibri
Structural changes caused by site-directed mutagenesis of tyrosine-98 in Desulfovibrio vulgaris flavodoxin delineated by 1H and 15N NMR spectroscopy: implications for redox potential modulation.
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Biochemistry. 1994 Dec 27;33(51):15298-308
Authors: Stockman BJ, Richardson TE, Swenson RP
Flavodoxins mediate electron transfer at low redox...
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[NMR paper] NMR-derived model for a peptide-antibody complex.
NMR-derived model for a peptide-antibody complex.
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Biochemistry. 1990 Oct 30;29(43):10032-41
Authors: Zilber B, Scherf T, Levitt M, Anglister J
The TE34 monoclonal antibody against cholera toxin peptide 3 (CTP3; VEVPGSQHIDSQKKA) was sequenced and investigated by two-dimensional transferred NOE difference spectroscopy and molecular modeling. The VH sequence of TE34, which does not bind cholera toxin, shares remarkable homology to that of TE32 and TE33, which are both anti-CTP3...
Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis,
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