Related ArticlesNMR observation of HIV-1 gp120 conformational flexibility resulting from V3 truncation.
FEBS J. 2014 Jul;281(13):3019-31
Authors: Moseri A, Schnur E, Noah E, Zherdev Y, Kessler N, Singhal Sinha E, Abayev M, Naider F, Scherf T, Anglister J
Abstract
The envelope spike of HIV-1, which consists of three external gp120 and three transmembrane gp41 glycoproteins, recognizes its target cells by successively binding to its primary CD4 receptor and a coreceptor molecule. Until recently, atomic-resolution structures were available primarily for monomeric HIV-1 gp120, in which the V1, V2 and V3 variable loops were omitted (gp120core ), in complex with soluble CD4 (sCD4). Differences between the structure of HIV gp120core in complex with sCD4 and the structure of unliganded simian immunodeficiency virus gp120core led to the hypothesis that gp120 undergoes a major conformational change upon sCD4 binding. To investigate the conformational flexibility of gp120, we generated two forms of mutated gp120 amenable for NMR studies: one with V1, V2 and V3 omitted ((mut) gp120core ) and the other containing the V3 region [(mut) gp120core (+V3)]. The TROSY-(1)H-(15)N-HSQC spectra of [(2)H, (13)C, (15)N]Arg-labeled and [(2)H, (13)C, (15)N]Ile-labeled unliganded (mut) gp120core showed many fewer crosspeaks than the expected number, and also many fewer crosspeaks in comparison with the labeled (mut) gp120core bound to the CD4-mimic peptide, CD4M33. This finding suggests that in the unliganded form, (mut) gp120core shows considerable flexibility and motions on the millisecond time scale. In contrast, most of the expected crosspeaks were observed for the unliganded (mut) gp120core (+V3), and only a few changes in chemical shift were observed upon CD4M33 binding. These results indicate that (mut) gp120core (+V3) does not show any significant conformational flexibility in its unliganded form and does not undergo any significant conformational change upon CD4M33 binding, underlining the importance of V3 in stabilizing the gp120core conformation.
Probing the HIV gp120 envelope glycoprotein conformation by NMR.
Probing the HIV gp120 envelope glycoprotein conformation by NMR.
Probing the HIV gp120 envelope glycoprotein conformation by NMR.
J Biol Chem. 2011 Jul 8;286(27):23975-81
Authors: Celigoy J, Ramirez B, Tao L, Rong L, Yan L, Feng YR, Quinnan GV, Broder CC, Caffrey M
Abstract
The HIV envelope glycoprotein gp120 plays a critical role in virus entry, and thus, its structure is of extreme interest for the development of novel therapeutics and vaccines. To date, high resolution structural information about gp120 in complex with gp41 has proven...
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09-09-2011 06:42 PM
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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08-30-2011 04:52 PM
NMR Provides a Quantitative Description of Protein Conformational Flexibility on Physiologically Important Timescales.
NMR Provides a Quantitative Description of Protein Conformational Flexibility on Physiologically Important Timescales.
NMR Provides a Quantitative Description of Protein Conformational Flexibility on Physiologically Important Timescales.
Biochemistry. 2011 Mar 9;
Authors: Salmon L, Bouvignies G, Markwick PR, Blackledge M
A complete description of biomolecular activity requires an understanding of the nature and the role of protein conformational dynamics. In recent years novel NMR-based techniques have emerged that provide hitherto inaccessible...
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03-11-2011 03:14 PM
[NMR paper] Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-
Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations.
Related Articles Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations.
J Pept Sci. 2004 Jun;10(6):363-80
Authors: Kanyalkar M, Srivastava S, Saran A, Coutinho E
The envelope proteins, gp 120 and gp41 of HIV-1, play a crucial role in receptor (CD4+ lymphocytes) binding and membrane fusion. The fragment 254-274 of gp120 is conserved in all strains of...
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11-24-2010 09:51 PM
[NMR paper] Expression, purification, and isotope labeling of a gp120 V3 peptide and production o
Expression, purification, and isotope labeling of a gp120 V3 peptide and production of a Fab from a HIV-1 neutralizing antibody for NMR studies.
Related Articles Expression, purification, and isotope labeling of a gp120 V3 peptide and production of a Fab from a HIV-1 neutralizing antibody for NMR studies.
Protein Expr Purif. 2002 Apr;24(3):374-83
Authors: Sharon M, Görlach M, Levy R, Hayek Y, Anglister J
Most human immunodeficiency virus type 1 (HIV-1) neutralizing antibodies in infected individuals and in immunized animals are directed...
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11-24-2010 08:49 PM
[NMR paper] NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
Related Articles NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
Biochemistry. 1998 Jul 28;37(30):10616-25
Authors: Gizachew D, Moffett DB, Busse SC, Westler WM, Dratz EA, Teintze M
A peptide containing residues 36-59 of the human CD4 receptor includes most of the residues thought to be involved in binding the HIV surface glycoprotein, gp120. This peptide was synthesized and inhibited the binding of gp120 to soluble CD4. NMR relaxation...
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11-17-2010 11:15 PM
[NMR paper] In vivo detection and characterization of protein adducts resulting from bioactivatio
In vivo detection and characterization of protein adducts resulting from bioactivation of haloethene cysteine S-conjugates by 19F NMR: chlorotrifluoroethene and tetrafluoroethene.
Related Articles In vivo detection and characterization of protein adducts resulting from bioactivation of haloethene cysteine S-conjugates by 19F NMR: chlorotrifluoroethene and tetrafluoroethene.
Chem Res Toxicol. 1992 Jan-Feb;5(1):34-41
Authors: Harris JW, Dekant W, Anders MW
Several haloalkenes are selective nephrotoxins. The bioactivation of nephrotoxic...
NMR observation of HIV-1 gp120 conformational flexibility resulting from V3 truncation.
Linear Mode
