Structural plasticity broadens the specificity of an engineered protease

作者: Roger Bone , Joy L. Silen , David A. Agard

DOI: 10.1038/339191A0

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摘要: The substrate specificity of α-lytic protease has been changed dramatically, with a concomitant increase in activity, by replacing an active-site Met Ala. both this mutant and another similar are extraordinarily broad. X-ray crystallographic analysis shows that structural plasticity, combination alternate side-chain conformations binding-site flexibility, allows large small substrates to be well accommodated.

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