Abstract：
: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.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Keller BG,Rademacher Cdoi
10.1016/j.sbi.2019.11.003subject
Has Abstractpub_date
2020-06-01 00:00:00pages
31-38eissn
0959-440Xissn
1879-033Xpii
S0959-440X(19)30123-Xjournal_volume
62pub_type
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journal_title：Current opinion in structural biology
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journal_title：Current opinion in structural biology
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