Allostery in C-type lectins.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
06 2020
06 2020
Historique:
received:
30
09
2019
revised:
30
10
2019
accepted:
04
11
2019
pubmed:
16
12
2019
medline:
23
7
2021
entrez:
16
12
2019
Statut:
ppublish
Résumé
C-type lectins are the largest and most diverse family of mammalian carbohydrate-binding proteins. They share a common protein fold, which provides the unifying basis for calcium-mediated carbohydrate recognition. Their involvement in a multitude of biological functions is remarkable. Here, we review the variety of tasks these lectins are involved in alongside with the structural demands on the overall protein architecture. Subtle changes of the protein structure are implemented to cope with such diverse functional requirements. The presence of a high level of structural dynamics over a broad palette of time scales is paired with the presence of secondary binding sites and allosteric coordination of remote sites and renders this lectin fold a highly adaptable scaffold.
Identifiants
pubmed: 31838280
pii: S0959-440X(19)30123-X
doi: 10.1016/j.sbi.2019.11.003
pii:
doi:
Substances chimiques
Lectins, C-Type
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
31-38Informations de copyright
Copyright © 2019. Published by Elsevier Ltd.