Zn-binding AZUL domain of human ubiquitin protein ligase Ube3A
Zn-binding AZUL domain of human ubiquitin protein ligase Ube3A
Abstract Ube3A (also referred to as E6AP for E6 Associated Protein) is a E3 ubiquitin-protein ligase implicated in the development of Angelman syndrome by controlling degradation of synaptic protein Arc and oncogenic papilloma virus infection by controlling degradation of p53. This article describe the solution NMR structure of the conserved N-terminal domain of human Ube3A (residues 24-87) that contains two residues (Cys44 and Arg62) found to be mutated in patients with Angelman syndrome. The structure of this domain...
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NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice.
NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice.
NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice.
Biomol NMR Assign. 2011 Apr 27;
Authors: Suzuki R, Tsuchiya W, Shindo H, Yamazaki T
The small ubiquitin-related modifier (SUMO) is a ubiquitin-like post-translational modifier that alters the localization, activity, or stability of many proteins. In the sumoylation process, an activated SUMO is transferred from SUMO-activating enzyme E1 complex (SAE1/SAE2) to...
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
Mol Biol Rep. 2010 Dec 12;
Authors: Paramanik V, Thakur MK
Nuclear magnetic resonance (NMR) spectroscopy is a useful biophysical technique to study the ligand-protein interaction. In this report, we have used bacterially produced ER? and its domains for studying the functional analysis of ligand-protein interaction....
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12-15-2010 12:03 PM
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Related Articles NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Biochemistry. 2010 Dec 1;
Authors: Lange A, Hoeller D, Wienk H, Marcillat O, Lancelin JM, Walker O
The VHS domain of the Stam2 protein is a ubiquitin binding domain involved in the recognition of ubiquitinated proteins committed to lysosomal degradation. Among all VHS domains, the VHS domain of Stam proteins is the strongest binder to...
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12-03-2010 08:52 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] Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shif
Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation.
Related Articles Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation.
Biochemistry. 1999 Jul 20;38(29):9242-53
Authors: Rajesh S, Sakamoto T, Iwamoto-Sugai M, Shibata T, Kohno T, Ito Y
The interaction between the 26 kDa yeast ubiquitin hydrolase (YUH1), involved in maintaining the monomeric ubiquitin pool in cells, and the 8.5 kDa yeast ubiquitin protein has been studied by heteronuclear...
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[NMR paper] NMR studies of the mode of binding of corepressors and inducers to Escherichia coli t
NMR studies of the mode of binding of corepressors and inducers to Escherichia coli trp repressor.
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 NMR studies of the mode of binding of corepressors and inducers to Escherichia coli trp repressor.
Eur J Biochem. 1996 Feb 1;235(3):804-13
Authors: Ramesh V, Syed SE, Frederick RO, Sutcliffe MJ, Barnes M, Roberts GC
The binding of the corepressors tryptophan and 5-methyltryptophan and...
NMR Reveals a Different Mode of Binding of the Stam2 VHS Domain to Ubiquitin and Diubiquitin,
Linear Mode
