Jian Zhu - Academia.edu (original) (raw)
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Papers by Jian Zhu
Journal of Biological Chemistry, 2012
Background: ADAMTS metalloproteases are multidomain proteins with remarkable substrate specificit... more Background: ADAMTS metalloproteases are multidomain proteins with remarkable substrate specificity. Results: Swapping noncatalytic domains between ADAMTS13 and ADAMTS5 causes reciprocal changes in the cleavage of their natural substrates. Conclusion: ADAMTS exosites in noncatalytic domains are portable modifiers of proteolytic activity. Significance: Shuffling and recombination of ADAMTS ancillary structural domains may be exploited to evolve or engineer new protease functions.
Journal of Biological Chemistry, 2012
Background: ADAMTS metalloproteases are multidomain proteins with remarkable substrate specificit... more Background: ADAMTS metalloproteases are multidomain proteins with remarkable substrate specificity. Results: Swapping noncatalytic domains between ADAMTS13 and ADAMTS5 causes reciprocal changes in the cleavage of their natural substrates. Conclusion: ADAMTS exosites in noncatalytic domains are portable modifiers of proteolytic activity. Significance: Shuffling and recombination of ADAMTS ancillary structural domains may be exploited to evolve or engineer new protease functions.