O-Linked glycans potentially play a functional role in cellular recognition events. Recent structural analyses suggest that O-glycosylation can be a specific signal for a lectin receptor which recognizes both the O-glycan and the adjacent polypeptide region. Further, certain antibodies specifically bind to the O-glycosylated peptide. There is growing interest in the mechanism by which O-glycans on proteins are specifically recognized by lectins and antibodies. The recognition system may be...
[NMR paper] O-Glycan-Dependent Interaction between MUC1 Glycopeptide and MY.1E12 Antibody by NMR, Molecular Dynamics and Docking Simulations
O-Glycan-Dependent Interaction between MUC1 Glycopeptide and MY.1E12 Antibody by NMR, Molecular Dynamics and Docking Simulations
Anti-mucin1 (MUC1) antibodies have been widely used for breast cancer diagnosis and treatment. This is based on the fact that MUC1 undergoes aberrant glycosylation upon cancer progression, and anti-MUC1 antibodies differentiate changes in glycan structure. MY.1E12 is a promising anti-MUC1 antibody with a distinct specificity toward MUC1 modified with an immature O-glycan (NeuAc?(2-3)Gal?(1-3)GalNAc) on a specific Thr. However, the structural basis for the...
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[NMR paper] Structural insights into the interaction of a monoclonal antibody and Nodal peptides by STD-NMR spectroscopy.
Structural insights into the interaction of a monoclonal antibody and Nodal peptides by STD-NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural insights into the interaction of a monoclonal antibody and Nodal peptides by STD-NMR spectroscopy.
Bioorg Med Chem. 2017 Dec 15;25(24):6589-6596
Authors: Calvanese L, Focà A, Sandomenico A, Focà G, Caporale A, Doti N, Iaccarino E, Leonardi A, D'Auria G, Ruvo M, Falcigno L
Abstract
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[NMR paper] Insights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.
Insights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Insights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.
J Med Chem. 2017 Jul 13;60(13):5749-5758
Authors: Gimeno A, Santos LM, Alemi M, Rivas J, Blasi D, Cotrina EY, Llop J,...
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[NMR paper] Solution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel ?4 subunit: A low affinity interaction is required for inhibition of Cav2.1 Ca2+ currents.
Solution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel ?4 subunit: A low affinity interaction is required for inhibition of Cav2.1 Ca2+ currents.
Solution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel ?4 subunit: A low affinity interaction is required for inhibition of Cav2.1 Ca2+ currents.
FASEB J. 2015 Jan 6;
Authors: Xu X, Zhang F, Zamponi GW, Horne WA
Abstract
Rem, Rad, Kir/Gem (RGK) proteins, including Rem2, mediate profound inhibition of high-voltage activated Ca(2+) channels...
[NMR paper] Solution NMR analysis of the interaction between the actinoporin Sticholysin I and DHPC micelles. Correlation with backbone dynamics.
Solution NMR analysis of the interaction between the actinoporin Sticholysin I and DHPC micelles. Correlation with backbone dynamics.
Related Articles Solution NMR analysis of the interaction between the actinoporin Sticholysin I and DHPC micelles. Correlation with backbone dynamics.
Proteins. 2013 Nov 12;
Authors: Castilla AL, Santos FP, Schreier S, Pires JR
Abstract
Sticholysin I (StI), an actinoporin expressed as a water-soluble protein by the sea anemone Stichodactyla helianthus, binds to natural and model membranes, forming oligomeric...
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[NMR paper] An NMR study of the interaction of 15N-labelled bradykinin with an antibody mimic of
An NMR study of the interaction of 15N-labelled bradykinin with an antibody mimic of the bradykinin B2 receptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles An NMR study of the interaction of 15N-labelled bradykinin with an antibody mimic of the bradykinin B2 receptor.
Eur J Biochem. 1997 Mar 1;244(2):471-8
Authors: Ottleben H, Haasemann M, Ramachandran R, Görlach M, Müller-Esterl W, Brown LR
An isotope-edited NMR study of...
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[NMR paper] An NMR study of the interaction of 15N-labelled bradykinin with an antibody mimic of
An NMR study of the interaction of 15N-labelled bradykinin with an antibody mimic of the bradykinin B2 receptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles An NMR study of the interaction of 15N-labelled bradykinin with an antibody mimic of the bradykinin B2 receptor.
Eur J Biochem. 1997 Mar 1;244(2):471-8
Authors: Ottleben H, Haasemann M, Ramachandran R, Görlach M, Müller-Esterl W, Brown LR
An isotope-edited NMR study of...
Solution NMR Analysis of O-Glycopeptide-Antibody Interaction
Linear Mode
