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PLoS One. 2014 Jun 17;9(6):e97198. doi: 10.1371/journal.pone.0097198. eCollection 2014.

Solution structure of the 2A protease from a common cold agent, human rhinovirus C2, strain W12.

Author information

1
National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
2
Institute for Molecular Virology, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
3
Center for Eukaryotic Structural Genomics, Biochemistry Department, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
4
National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison, Madison, Wisconsin, United States of America; Center for Eukaryotic Structural Genomics, Biochemistry Department, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.

Abstract

Human rhinovirus strains differ greatly in their virulence, and this has been correlated with the differing substrate specificity of the respective 2A protease (2Apro). Rhinoviruses use their 2Apro to cleave a spectrum of cellular proteins important to virus replication and anti-host activities. These enzymes share a chymotrypsin-like fold stabilized by a tetra-coordinated zinc ion. The catalytic triad consists of conserved Cys (C105), His (H34), and Asp (D18) residues. We used a semi-automated NMR protocol developed at NMRFAM to determine the solution structure of 2Apro (C105A variant) from an isolate of the clinically important rhinovirus C species (RV-C). The backbone of C2 2Apro superimposed closely (1.41-1.81 Å rmsd) with those of orthologs from RV-A2, coxsackie B4 (CB4), and enterovirus 71 (EV71) having sequence identities between 40% and 60%. Comparison of the structures suggest that the differential functional properties of C2 2Apro stem from its unique surface charge, high proportion of surface aromatics, and sequence surrounding the di-tyrosine flap.

PMID:
24937088
PMCID:
PMC4061012
DOI:
10.1371/journal.pone.0097198
[Indexed for MEDLINE]
Free PMC Article
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