Related ArticlesEpitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by saturation transfer difference NMR spectroscopy.
Biochem Biophys Res Commun. 2003 Aug 1;307(3):498-502
Authors: Murata T, Hemmi H, Nakajima M, Yoshida M, Yamaguchi I
Saturation transfer difference (STD) NMR spectroscopy is a promising tool for rapid screening, identifying ligands that interact with a target protein, and characterizing the epitopes of the ligands. Gibberellins (GAs) are a class of plant hormones and form a large family consisting of more than 120 members. A few of them, called "active" GAs, are considered to be perceptible to a receptor that remains unknown. We applied STD NMR spectroscopy to detect the binding activity and identify the binding epitope of gibberellin A(3) (GA(3)) that is recognized by monoclonal antibody 4-B8(8)/E9. This is one of the antibodies that can mimic a GA receptor in the manner of recognition of active GAs. The information on the binding epitope, obtained by STD NMR, was in good agreement with that shown by analyzing the crystal structure of the antibody-GA(4) complex. This suggests that STD NMR spectroscopy would be very useful to characterize the interaction between GAs and such binding proteins as GA-catabolic enzymes and receptors.
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Feb 1;17(5):1547-1560
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-),...
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01-27-2011 02:52 PM
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Jan 5;
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-), with the broadly...
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01-06-2011 11:21 AM
[NMR paper] Epitope mapping of the phosphorylation motif of the HIV-1 protein Vpu bound to the se
Epitope mapping of the phosphorylation motif of the HIV-1 protein Vpu bound to the selective monoclonal antibody using TRNOESY and STD NMR spectroscopy.
Related Articles Epitope mapping of the phosphorylation motif of the HIV-1 protein Vpu bound to the selective monoclonal antibody using TRNOESY and STD NMR spectroscopy.
Biochemistry. 2004 Nov 23;43(46):14555-65
Authors: Gharbi-Benarous J, Bertho G, Evrard-Todeschi N, Coadou G, Megy S, Delaunay T, Benarous R, Girault JP
The conformational preferences of a 22-amino acid peptide...
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11-24-2010 10:03 PM
[NMR paper] Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion
Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion measurements.
Related Articles Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion measurements.
J Am Chem Soc. 2004 Nov 3;126(43):14258-66
Authors: Lucas LH, Price KE, Larive CK
It is important to characterize drug-albumin binding during drug discovery and lead optimization as strong binding may reduce bioavailability and/or increase the drug's in vivo half-life. Despite knowing about the location of human serum albumin (HSA)...
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11-24-2010 10:03 PM
[NMR paper] Epitope mapping of ligand-receptor interactions by diffusion NMR.
Epitope mapping of ligand-receptor interactions by diffusion NMR.
Related Articles Epitope mapping of ligand-receptor interactions by diffusion NMR.
J Am Chem Soc. 2002 Aug 28;124(34):9984-5
Authors: Yan J, Kline AD, Mo H, Zartler ER, Shapiro MJ
A novel method based on diffusion NMR for the epitope mapping of ligand binding is presented. The intermolecular NOE builds up during a long diffusion period and creates a deviation from the linearity. The ligand proton nearest the protein generates the strongest NOE from protein during the diffusion...
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11-24-2010 08:58 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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11-19-2010 08:32 PM
[NMR paper] NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface i
NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.
Related Articles NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.
Structure. 2000 Apr 15;8(4):385-95
Authors: Tugarinov V, Zvi A, Levy R, Hayek Y, Matsushita S, Anglister J
BACKGROUND: The protein 0.5beta is a potent strain-specific human immunodeficiency virus type 1 (HIV-1) neutralizing antibody raised against the entire envelope glycoprotein (gp120) of...
Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by sa
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