Interferon-stimulated gene-15 (ISG15) is an interferon-induced protein with two ubiquitin-like (Ubl) domains linked by a short peptide chain and is a conjugated protein of the ISGylation system. Similar to ubiquitin and other Ubls, ISG15 is ligated to its target proteins through a series of E1, E2, and E3 enzymes known as Uba7, Ube2L6/UbcH8, and HERC5, respectively. Ube2L6/UbcH8 plays a central role in ISGylation, underscoring it as an important drug target for boosting innate antiviral...
[NMR paper] Characterizing the monomer-dimer equilibrium of UbcH8/Ube2L6: A combined SAXS and NMR study
Characterizing the monomer-dimer equilibrium of UbcH8/Ube2L6: A combined SAXS and NMR study
Interferon-stimulated gene-15 (ISG15) is an interferon-induced protein with two ubiquitin-like (Ubl) domains linked by a short peptide chain, and the conjugated protein of the ISGylation system. Similar to ubiquitin and other Ubls, ISG15 is ligated to its target proteins with a series of E1, E2, and E3 enzymes known as Uba7, Ube2L6/UbcH8, and HERC5, respectively. Ube2L6/UbcH8 plays a literal central role in ISGylation, underscoring it as an important drug target for boosting innate antiviral...
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04-25-2023 01:59 PM
[NMR paper] NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of Helicobacter pylori (Hup).
NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of Helicobacter pylori (Hup).
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of Helicobacter pylori (Hup).
Magn Reson Chem. 2017 Dec 14;:
Authors: Jaiswal N, Raikwal N, Pandey H, Agarwal N, Arora A, Poluri KM, Kumar D
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12-15-2017 09:07 PM
[NMR paper] Human ?B2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.
Human ?B2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.
Related Articles Human ?B2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.
Structure. 2017 Feb 16;:
Authors: Xi Z, Whitley MJ, Gronenborn AM
Abstract
??-Crystallins are long-lived eye lens proteins that are crucial for lens transparency and refractive power. Each ??-crystallin comprises two homologous domains, which are connected by a short linker. ?-Crystallins are monomeric, while ?-crystallins...
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02-28-2017 12:29 PM
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been implicated in the pathophysiology of various diseases including chronic obstructive pulmonary disease (COPD) and cancer. CXCL8 exists as monomers and dimers but monomer alone binds CXCR1 with high affinity. CXCL8 function involves binding two distinct CXCR1 sites – the N-terminal domain (Site-I) and the extracellular/transmembrane domain (Site-II). Therefore, higher monomer affinity...
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11-28-2014 11:37 AM
[NMR paper] Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
Protein Sci. 2014 Oct 18;
Authors: Joseph PR, Rajarathnam K
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been...
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10-21-2014 11:31 PM
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been implicated in the pathophysiology of various diseases including chronic obstructive pulmonary disease (COPD) and cancer. CXCL8 exists as monomers and dimers but monomer alone binds CXCR1 with high affinity. CXCL8 function involves binding two distinct CXCR1 sites – the N-terminal domain (Site-I) and the extracellular/transmembrane domain (Site-II). Therefore, higher monomer affinity...
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10-18-2014 09:26 PM
TransientElectrostatic Interactions Dominate theConformational Equilibrium Sampled by Multidomain Splicing FactorU2AF65: A Combined NMR and SAXS Study
TransientElectrostatic Interactions Dominate theConformational Equilibrium Sampled by Multidomain Splicing FactorU2AF65: A Combined NMR and SAXS Study
Jie-rong Huang, Lisa R. Warner, Carolina Sanchez, Frank Gabel, Tobias Madl, Cameron D. Mackereth, Michael Sattler and Martin Blackledge
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja502030n/aop/images/medium/ja-2014-02030n_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja502030n
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04-30-2014 02:03 AM
[NMR paper] Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
Related Articles Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
J Am Chem Soc. 2014 Apr 16;
Authors: Huang JR, Warner LR, Sanchez C, Gabel F, Madl T, Mackereth CD, Sattler M, Blackledge M
Abstract
Multi-domain proteins containing intrinsically disordered linkers exhibit...
Characterizing the Monomer-Dimer Equilibrium of UbcH8/Ube2L6: A Combined SAXS and NMR Study
Linear Mode
