The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (M-pro)

Ali Ebrahim,Blake T. Riley,Desigan Kumaran,Babak Andi,Martin R. Fuchs,Sean McSweeney,Daniel A. Keedy

bioRxiv : the preprint server for biology（2021）

引用 22|浏览8

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摘要

X-ray crystallography at variable temperature for SARS-CoV-2 M reveals a complex conformational landscape, including mobile solvent at the catalytic dyad, mercurial conformational heterogeneity in a key substrate-binding loop, and an intramolecular network bridging the active site and dimer interface.

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关键词

SARS-CoV-2,X-ray crystallography,multitemperature crystallography,protein structure,protein flexibility

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