Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10.
Biochemistry
Biochemistry Methods
Data Analysis in Structural Biology
Structural Biology
Journal
iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038
Informations de publication
Date de publication:
26 Jun 2020
26 Jun 2020
Historique:
received:
17
04
2020
revised:
20
05
2020
accepted:
29
05
2020
entrez:
8
7
2020
pubmed:
8
7
2020
medline:
8
7
2020
Statut:
ppublish
Résumé
Siglec-10 is an inhibitory I-type lectin selectively recognizing sialoglycans exposed on cell surfaces, involved in several patho-physiological processes. The key role Siglec-10 plays in the regulation of immune cell functions has made it a potential target for the development of immunotherapeutics against a broad range of diseases. However, the crystal structure of the protein has not been resolved for the time being and the atomic description of Siglec-10 interactions with complex glycans has not been previously unraveled. We present here the first insights of the molecular mechanisms regulating the interaction between Siglec-10 and naturally occurring sialoglycans. We used combined spectroscopic, computational and biophysical approaches to dissect glycans' epitope mapping and conformation upon binding in order to afford a description of the 3D complexes. Our outcomes provide a structural perspective for the rational design and development of high-affinity ligands to control the receptor functionality.
Identifiants
pubmed: 32629603
pii: S2589-0042(20)30416-8
doi: 10.1016/j.isci.2020.101231
pmc: PMC7306591
pii:
doi:
Types de publication
Journal Article
Langues
eng
Pagination
101231Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Commentaires et corrections
Type : ErratumIn
Informations de copyright
Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Interests The authors declare no competing interests.
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