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
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

31-38

Informations de copyright

Copyright © 2019. Published by Elsevier Ltd.

Auteurs

Bettina G Keller (BG)

Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, 14195 Berlin, Germany.

Christoph Rademacher (C)

Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, 14195 Berlin, Germany; Max Planck Institute of Colloids and Interfaces, Department of Biomolecular Systems, 14424 Potsdam, Germany. Electronic address: christoph.rademacher@mpikg.mpg.de.

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Classifications MeSH