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Foldon unfolding mediates the interconversion between M(pro)-C monomer and 3D domain-swapped dimer.

Proceedings of the National Academy of Sciences of the United States of America - 11 Sept 2012

Kang Xue, Zhong Nan, Zou Peng, Zhang Shengnan, Jin Changwen, Xia Bin

Abstract excerpt

The C-terminal domain (M(pro)-C) of SARS-CoV main protease adopts two different fold topologies, a monomer and a 3D domain-swapped dimer. Here, we report that M(pro)-C can reversibly interconvert between these two topological states under physiological conditions. Although the swapped α(1)-helix is fully buried inside the protein hydrophobic core, the interconversion of M(pro)-C is carried out without the...

Topics

Circular Dichroism
Coronavirus 3C Proteases
Cysteine Endopeptidases
Dimerization
Kinetics
Magnetic Resonance Spectroscopy
Mutagenesis
Mutation
Protein Conformation
Protein Folding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Thermodynamics

Viral Proteins

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Identifiers

PMID: 22927388
DOI: 10.1073/pnas.1205241109
PMCID: PMC3443179

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