[NMR paper] NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of Helicobacter pylori (Hup).
Related ArticlesNMR 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
Abstract
Helicobacter pylori (H. pylori) colonizes under harsh acidic/oxidative stress conditions of human gastrointestinal tract and can survive there for infinitely longer durations of host life. The bacterium expresses several harbinger proteins to facilitate its persistent colonization under such conditions. One such protein in H. pylori is Histone like DNA binding protein (Hup) which in its homo-dimeric form binds to DNA to perform various DNA dependent cellular activities. Further, it also plays an important role in protecting the genomic DNA from oxidative stress and acidic denaturation. Legitimately, if the binding of Hup to DNA is suppressed, it will directly impact on the survival of the bacterium, thus making Hup a potential therapeutic target for developing new anti-H. pylori agents. However, to inhibit the binding of Hup to DNA, it is necessary to gain detailed insights into the molecular and structural basis of Hup-dimerization and its binding mechanism to DNA. As a first step in this direction, we report here the NMR assignments and structural features of Hup at pH 6.0. The study revealed the occurrence of dynamic equilibrium between its monomer and dimer conformations. The dynamic equilibrium was found to shifting towards dimer both at low temperature and pH; whereas DNA binding studies evidenced that the protein binds to DNA in its dimeric form. These preliminary investigations correlate very well with the diverse functionality of protein and will form the basis for future studies aiming to develop novel anti-H. pylori agents employing structure-based-rational drug discovery approach.
PMID: 29241299 [PubMed - as supplied by publisher]
[NMR paper] Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates differential binding interactions.
Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates differential binding interactions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-highwire.gif 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 Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates...
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04-02-2016 09:55 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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[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
[NMR paper] NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
Related Articles NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
Biomol NMR Assign. 2013 Jul 4;
Authors: Chien CT, Wang LW, Liu YN, Hsu BD, Lyu PC, Hsu ST
Abstract
Many knotted proteins have been discovered recently, but the folding process of which remains elusive. HP0242 is a hypothetical protein from Helicobacter pylori, which is a model system for studying the folding pathway of a knotted protein. In...
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07-05-2013 09:52 PM
[NMR paper] Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Protein Expr Purif. 2013 Feb 27;
Authors: Fuengfuloy P, Chuawong P, Suebka S, Wattana-Amorn P, Williams C, Crump MP, Songsiriritthigul C
Abstract
Aminoacyl-tRNA synthetases (aaRSs) covalently...
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03-05-2013 03:25 PM
[NMR paper] The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
Dalton Trans. 2013 Jan 21;
Authors: Rowinska-Zyrek M, Potocki S, Witkowska D, Valensin D, Kozlowski H
Abstract
HypA, a nickel accessory protein from H. pylori, binds a zinc ion in it's structural site, a loop with two conserved...
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[NMR paper] NMR assignment of the novel Helicobacter pylori protein JHP1348.
NMR assignment of the novel Helicobacter pylori protein JHP1348.
Related Articles NMR assignment of the novel Helicobacter pylori protein JHP1348.
J Biomol NMR. 2005 Jul;32(3):262
Authors: Borin BN, Popescu A, Krezel AM
NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of Helicobacter pylori (Hup).
Linear Mode
