Related ArticlesCo-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR.
Protein Expr Purif. 2017 Jul 24;:
Authors: Woestenenk E, Agback P, Unnerstċle S, Henderson I, Agback T
Abstract
A novel approach for separate expression of dengue virus NS3 protease and its NS2B cofactor domain is described in this paper. The two proteins are expressed in E.coli and purified separately and subsequently efficiently co-refolded to form a stable complex. This straightforward and robust method allows for separate isotope labeling of the two proteins, facilitating analysis by nuclear magnetic resonance (NMR) spectroscopy. Unlinked NS2B-NS3pro behaves better in NMR spectroscopy than linked NS2B-NS3pro, which has resulted in the backbone resonance assignment of the unlinked NS2B-NS3 complex bound to a peptidic boronic acid inhibitor.
PMID: 28751017 [PubMed - as supplied by publisher]
[NMR paper] Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.
Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.
Related Articles Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.
Biomol NMR Assign. 2017 Feb 28;:
Authors: Conroy BS, Weiss ER, Smith SP, Langelaan DN
Abstract
Krüppel-like factor 4 (KLF4) is a transcription factor involved in diverse biological processes, including development, cellular differentiation and proliferation, and maintenance of tissue homeostasis. KLF4 has...
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03-02-2017 04:07 PM
[NMR paper] NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
Biomol NMR Assign. 2016 Jun 29;
Authors: Amin N, Nietlispach D, Qamar S, Coyle J, Chiarparin E, Williams G
Abstract
Proteins of the NSD family are histone-methyl transferases with critical functions in the regulation of chromatin structure and function. NSD1 and NSD2 are homologous proteins that function as epigenetic...
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07-01-2016 03:22 PM
[NMR paper] NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests...
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05-24-2016 11:36 AM
[NMR paper] Conformational change study of dengue virus NS2B-NS3 protease using 19F NMR spectroscopy.
Conformational change study of dengue virus NS2B-NS3 protease using 19F NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Conformational change study of dengue virus NS2B-NS3 protease using 19F NMR spectroscopy.
Biochem Biophys Res Commun. 2015 Jun 12;461(4):677-80
Authors: Zhu L, Yang J, Li H, Sun H, Liu J, Wang J
Abstract
The dengue virus NS2B-NS3 protease (NS2B-NS3p), an important antiviral target for drug development,...
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08-02-2015 07:10 AM
[NMR paper] Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy.
Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy.
Related Articles Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy.
Biochim Biophys Acta. 2015 Jun 11;
Authors: Li Y, Li Q, Wong YL, Liew LS, Kang C
Abstract
Non-structural (NS) proteins of dengue virus (DENV) are important for viral replication. There are four membrane proteins that are coded by viral genome. NS2B was shown to be one of the membrane proteins and its main function was confirmed to regulate viral protease activity. Its...
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06-15-2015 02:45 PM
[NMR paper] NMR study of non-structural proteins-part I: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Mayaro virus (MAYV).
NMR study of non-structural proteins-part I: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Mayaro virus (MAYV).
Related Articles NMR study of non-structural proteins-part I: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Mayaro virus (MAYV).
Biomol NMR Assign. 2014 Sep 13;
Authors: Melekis E, Tsika AC, Lichière J, Chasapis CT, Margiolaki I, Papageorgiou N, Coutard B, Bentrop D, Spyroulias GA
Abstract
Macro domains are ADP-ribose-binding modules present...
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09-14-2014 02:26 PM
[NMR paper] NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
Related Articles NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
J Biol Chem. 2013 Mar 19;
Authors: Kim YM, Gayen S, Kang C, Joy J, Huang Q, Chen AS, Wee JL, Ang MJ, Lim HA, Hung AW, Li R, Noble CG, Lee LT, Yip A, Wang QY, Chia CS, Hill J, Shi PY, Keller TH
Abstract
The dengue virus (DENV) is a mosquito-borne pathogen responsible for an estimated 100 million human infections annually. The viral genome encodes a...
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03-21-2013 02:58 PM
[NMR paper] Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by
Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.
Biochemistry. 1996 Oct 1;35(39):12694-704
Authors: Wang YX, Freedberg DI, Grzesiek S, Torchia DA, Wingfield PT, Kaufman JD, Stahl SJ, Chang CH, Hodge CN
A tetrahedrally hydrogen-bonded structural water molecule, water 301, is seen in...
Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR.
Linear Mode
