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Article

Receptor-binding loops in alphacoronavirus adaptation and evolution.

Nature communications - 23 Nov 2017

Wong Alan H M, Tomlinson Aidan C A, Zhou Dongxia, Satkunarajah Malathy, Chen Kevin, Sharon Chetna, Desforges Marc, Talbot Pierre J, Rini James M

Abstract excerpt

RNA viruses are characterized by a high mutation rate, a buffer against environmental change. Nevertheless, the means by which random mutation improves viral fitness is not well characterized. Here we report the X-ray crystal structure of the receptor-binding domain (RBD) of the human coronavirus, HCoV-229E, in complex with the ectodomain of its receptor, aminopeptidase N (APN). Three extended loops are solely...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 29170370
DOI: 10.1038/s41467-017-01706-x
PMCID: PMC5701055

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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