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 intractable. In this study, we characterize the structural properties of gp120 in the presence and absence of gp41 domains by NMR. Using the peptide probe 12p1 (sequence, RINNIPWSEAMM), which was identified previously as an entry inhibitor that binds to gp120, we identify atoms of 12p1 in close contact with gp120 in the monomeric and trimeric states. Interestingly, the binding mode of 12p1 with gp120 is similar for clades B and C. In addition, we show a subtle difference in the binding mode of 12p1 in the presence of gp41 domains, i.e. the trimeric state, which we interpret as small differences in the gp120 structure in the presence of gp41.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
J Biomol NMR. 2011 Jun 12;
Authors: Sastry M, Xu L, Georgiev IS, Bewley CA, Nabel GJ, Kwong PD
NMR spectroscopic characterization of the structure or the dynamics of proteins generally requires the production of samples isotopically enriched in (15)N, (13)C, or (2)H. The bacterial expression systems currently in use to...
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06-15-2011 01:15 PM
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
Abstract NMR spectroscopic characterization of the structure or the dynamics of proteins generally requires the production of samples isotopically enriched in 15N, 13C, or 2H. The bacterial expression systems currently in use to obtain isotopic enrichment, however, cannot produce a number of eukaryotic proteins, especially those that require post-translational modifications such as N-linked glycosylation for proper folding or activity. Here, we report the use of an...
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06-15-2011 02:31 AM
[NMR paper] NMR assignment of the vaccinia virus envelope protein A27L.
NMR assignment of the vaccinia virus envelope protein A27L.
Related Articles NMR assignment of the vaccinia virus envelope protein A27L.
J Biomol NMR. 2005 Jun;32(2):178
Authors: Chu FI, Ho Y, Tzou DL
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11-25-2010 08:21 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] Structural analysis of the extracellular domain of vaccinia virus envelope protein, A
Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
Related Articles Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
J Biol Chem. 2002 Jun 7;277(23):20949-59
Authors: Lin TH, Chia CM, Hsiao JC, Chang W, Ku CC, Hung SC, Tzou DL
This study presents the molecular structure of the extracellular domain of vaccinia virus envelope protein, A27L, determined by NMR and CD spectroscopy. A recombinant protein, eA27L-aa,...
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11-24-2010 08:49 PM
[NMR paper] Probing the conformation of the sugar transport inhibitor phlorizin by 2D-NMR, molecu
Probing the conformation of the sugar transport inhibitor phlorizin by 2D-NMR, molecular dynamics studies, and pharmacophore analysis.
Related Articles Probing the conformation of the sugar transport inhibitor phlorizin by 2D-NMR, molecular dynamics studies, and pharmacophore analysis.
J Med Chem. 2000 May 4;43(9):1692-8
Authors: Wielert-Badt S, Lin JT, Lorenz M, Fritz S, Kinne RK
Sodium/D-glucose cotransport, one of the prototypes for sodium gradient-driven symport systems in kidney and intestine, is known to be inhibited by aromatic and...
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11-18-2010 09:15 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] 1H- and natural abundance 15N-NMR studies of a derivative of a rabies glycoprotein fr
1H- and natural abundance 15N-NMR studies of a derivative of a rabies glycoprotein fragment.
Related Articles 1H- and natural abundance 15N-NMR studies of a derivative of a rabies glycoprotein fragment.
Biopolymers. 1991 May;31(6):713-23
Authors: Molinari H, Consonni R, Pegna M, Zetta L, Neri P, Niccolai N, Bonci A, Lozzi L, Rustici M, Scarselli M
Using a combination of one- and two-dimensional methods, 1H- and 15N-nmr spectroscopy has been employed to perform the complete assignment and the structural determination of the immunogenic...
Probing the HIV gp120 envelope glycoprotein conformation by NMR.
Linear Mode
