A fresh trim provides a new look at the human mannose receptor.
Ontology highlight
ABSTRACT: The human mannose receptor plays an important role in scavenging a variety of glycans and glycoconjugates, which contributes to both innate and adaptive immunity. However, the fine details of its ligand specificity, and specifically that of carbohydrate-recognition domain 4, the most functionally relevant C-type lectin domain within the receptor, are not completely understood. Feinberg et al. use glycan arrays, crystallography, and a newly trimmed version of carbohydrate-recognition domain 4 to elucidate the molecular mechanisms driving binding specificity. These data contribute to our molecular understanding of Ca2+-mediated binding promiscuity in the human mannose receptor and the scavenging role of the receptor itself and highlight unexpected interactions that should inspire further study.
SUBMITTER: Ficko-Blean E
PROVIDER: S-EPMC8294574 | biostudies-literature |
REPOSITORIES: biostudies-literature
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