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Article

Structural basis for receptor-binding domain mobility of the spike in SARS-CoV-2 BA.2.86 and JN.1.

Nature communications - 7 Oct 2024

Yajima Hisano, Anraku Yuki, Kaku Yu, Kimura Kanako Terakado, Plianchaisuk Arnon, Okumura Kaho, Nakada-Nakura Yoshiko, Atarashi Yusuke, Hemmi Takuya, Kuroda Daisuke, Takahashi Yoshimasa, Kita Shunsuke, Sasaki Jiei, Sumita Hiromi, Ito Jumpei, Maenaka Katsumi, Sato Kei, Hashiguchi Takao

Abstract excerpt

Since 2019, SARS-CoV-2 has undergone mutations, resulting in pandemic and epidemic waves. The SARS-CoV-2 spike protein, crucial for cellular entry, binds to the ACE2 receptor exclusively when its receptor-binding domain (RBD) adopts the up-conformation. However, whether ACE2 also interacts with the RBD in the down-conformation to facilitate the conformational shift to RBD-up remains unclear. Herein, we present...

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Share to Angiotensin-Converting Enzyme 2
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 39375326
DOI: 10.1038/s41467-024-52808-2
PMCID: PMC11458767

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

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