Related ArticlesThe C4 region as a target for HIV entry inhibitors--NMR mapping of the interacting segments of T20 and gp120.
FEBS J. 2015 Dec;282(24):4643-57
Authors: Moseri A, Biron Z, Arshava B, Scherf T, Naider F, Anglister J
Abstract
The peptide T20, which corresponds to a sequence in the C-terminal segment of the HIV-1 transmembrane glycoprotein gp41, is a strong entry inhibitor of HIV-1. It has been assumed that T20 inhibits HIV-1 infection by binding to the trimer formed by the N-terminal helical region (HR1) of gp41, preventing the formation of a six helix bundle by the N- and C-terminal helical regions of gp41. In addition to binding to gp41, T20 was found to bind to gp120 of X4 viruses and this binding was suggested to be responsible for an alternative mechanism of HIV-1 inhibition by this peptide. In the present study, T20 also was found to bind R5 gp120. Using NMR spectroscopy, the segments of T20 that interact with both gp120 and a gp120/CD4M33 complex were mapped. A peptide corresponding to the fourth constant region of gp120, sC4, was found to partially recapitulate gp120 binding to T20 and the segment of this peptide interacting with T20 was mapped. The present study concludes that an amphiphilic helix on the T20 C-terminus binds through mostly hydrophobic interactions to a nonpolar gp120 surface formed primarily by the C4 region. The ten- to thousand-fold difference between the EC50 of T20 against viral fusion and the affinity of T20 to gp120 implies that binding to gp120 is not a major factor in T20 inhibition of HIV-1 fusion. Nevertheless, this hydrophobic gp120 surface could be a target for anti-HIV therapeutics.
[NMR paper] The soluble Y115E-Y117E variant of human glutaminyl cyclase is a valid target for X-ray and NMR screening of inhibitors against Alzheimer disease.
The soluble Y115E-Y117E variant of human glutaminyl cyclase is a valid target for X-ray and NMR screening of inhibitors against Alzheimer disease.
Related Articles The soluble Y115E-Y117E variant of human glutaminyl cyclase is a valid target for X-ray and NMR screening of inhibitors against Alzheimer disease.
Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):986-92
Authors: DiPisa F, Pozzi C, Benvenuti M, Andreini M, Marconi G, Mangani S
Abstract
Recent developments in molecular pathology and genetics have allowed the...
[NMR paper] NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
Related Articles NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
FEBS J. 2013 Mar 8;
Authors: Schnur E, Kessler N, Zherdev Y, Noah E, Scherf T, Ding FX, Rabinovich S, Arshava B, Kurbatska V, Leonciks A, Tsimanis A, Rosen O, Naider F, Anglister J
Abstract
Chemokines constitute a large family of small proteins that regulate leukocyte trafficking to the site of inflammation by binding to specific cell-surface...
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NMR Structure and Dynamics of the C-Terminal Domain from Human Rev1 and Its Complex with Rev1 Interacting Region of DNA Polymerase ?
NMR Structure and Dynamics of the C-Terminal Domain from Human Rev1 and Its Complex with Rev1 Interacting Region of DNA Polymerase ?
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi300566z/aop/images/medium/bi-2012-00566z_0004.gif
Biochemistry
DOI: 10.1021/bi300566z
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06-29-2012 08:44 AM
[NMR paper] Mapping the interacting regions between troponins T and C. Binding of TnT and TnI pep
Mapping the interacting regions between troponins T and C. Binding of TnT and TnI peptides to TnC and NMR mapping of the TnT-binding site on TnC.
Related Articles Mapping the interacting regions between troponins T and C. Binding of TnT and TnI peptides to TnC and NMR mapping of the TnT-binding site on TnC.
J Biol Chem. 2001 Sep 28;276(39):36606-12
Authors: Blumenschein TM, Tripet BP, Hodges RS, Sykes BD
Muscular contraction is triggered by an increase in calcium concentration, which is transmitted to the contractile proteins by the troponin...
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11-19-2010 08:44 PM
[NMR paper] Group epitope mapping by saturation transfer difference NMR to identify segments of a
Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor.
Related Articles Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor.
J Am Chem Soc. 2001 Jun 27;123(25):6108-17
Authors: Mayer M, Meyer B
A protocol based on saturation transfer difference (STD) NMR spectra was developed to characterize the binding interactions at an atom level, termed group epitope mapping (GEM). As an example...
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[NMR paper] Mapping the cytochrome c553 interacting site using 1H and 15N NMR.
Mapping the cytochrome c553 interacting site using 1H and 15N NMR.
Related Articles Mapping the cytochrome c553 interacting site using 1H and 15N NMR.
FEBS Lett. 1999 Oct 22;460(1):77-80
Authors: Morelli X, Guerlesquin F
Cytochrome c553 is the electron transfer partner of formate dehydrogenase and of
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[NMR images] View this protein\x26#39;s PDB entry
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