August 15, 1996Biochemical JournalOpen Access

Human rhinovirus 2A proteinase mutant and its second-site revertants

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Population

Human rhinovirus 2A proteinase expressed in Escherichia coli strain BL21(DE3)

Comparison

Mutations in 2A proteinase vs Wild-type 2A proteinase

Design

Preclinical

Authors

MLMarion LUDERER-GMACH HLHans‐Dieter LiebigMedical University of Vienna WSWolfgang SommergruberFH Campus Wien

Discussion

Member takes

Implication

Mutant stability shifts confirm key C-terminal interactions in rhinoviral 2A; leaves open any therapeutic protein-engineering applications.

Structured PICO

Population

Human rhinovirus 2A proteinase expressed in Escherichia coli strain BL21(DE3)

Intervention

Mutations in 2A proteinase (Phe-130-->Tyr and second-site revertants His-135-->Arg or His-137-->Arg)

Comparator

Wild-type 2A proteinase

Outcome

Enzyme activity and structural stability (thermal transition temperatures)surrogate

Essential interactions exist within the C-terminal domain of human rhinoviral 2A proteinases that contribute to the overall stability and integrity of the enzyme.

Cite This Study

LUDERER-GMACH et al. (1996) studied this question.

synapsesocial.com/papers/6a8d0666d190ea52f78e4d9b https://doi.org/10.1042/bj3180213

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Implication

Mutant stability shifts confirm key C-terminal interactions in rhinoviral 2A; leaves open any therapeutic protein-engineering applications.