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Structures of the Inhibitory Receptor Siglec-8 in Complex with a High-Affinity Sialoside Analogue and a Therapeutic Antibody

María Pia Lenza, Unai Atxabal, Corwin M. Nycholat, Iker Oyenarte, Antonio Franconetti, Jon I. Quintana, Sandra Delgado, Reyes Núñez‐Franco, Carmen Teresa Garnica Marroquín, Helena Coelho, Luca Unione, Gonzalo Jiménez‐Osés, Filipa Marcelo, Mario Schubert, James C. Paulson, Jesús Jiménez‐Barbero, June Ereño‐Orbea

2022JACS Au19 citationsDOIOpen Access PDF

Abstract

' loop. The results reveal the basis for the observed high affinity of this ligand and provide clues for the rational design of the next generation of Siglec-8 inhibitors. Additionally, the specific interactions between Siglec-8 and the N-linked glycans present on the high-affinity receptor FcεRIα have also been explored by NMR.

Topics & Concepts

SIGLECDegranulationMonoclonal antibodyReceptorChemistryCD22AntibodySialic acidMast cellCell biologyBiochemistryBiologyImmunologyGlycosylation and Glycoproteins ResearchMonoclonal and Polyclonal Antibodies ResearchMast cells and histamine
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