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

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. The...

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Veröffentlicht in:	PloS one 2014-06, Vol.9 (6), p.e97198-e97198
Hauptverfasser:	Lee, Woonghee, Watters, Kelly E, Troupis, Andrew T, Reinen, Nichole M, Suchy, Fabian P, Moyer, Kylie L, Frederick, Ronnie O, Tonelli, Marco, Aceti, David J, Palmenberg, Ann C, Markley, John L
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aromatic compounds Aromatics Automation Biochemistry Biology and life sciences Catalysis Chymotrypsin Common cold Cysteine Endopeptidases - chemistry Enzymes Genomes Genomics Infections Magnetic Resonance Spectroscopy Molecular Sequence Data NMR Nuclear magnetic resonance Protease Protein Structure, Tertiary Proteinase Proteins Proteomics Research and analysis methods Rhinovirus Rhinovirus - enzymology Substrate specificity Substrates Surface charge Tyrosine Viral Proteins - chemistry Virology Virulence Viruses Zinc
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