Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain (Q27635416)

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A Kadziola

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C Lauritzen

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J Pedersen

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S Larsen

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S W Dahl

Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo

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language of work or name

English

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publication date

12 October 2001

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published in

FEBS Letters

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volume

506

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issue

3

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page(s)

201-6

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cites work

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Oligomeric structure and substrate induced inhibition of human cathepsin C

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Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing

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Purification and characterization of cathepsin J from rat liver

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Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C

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Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S.

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Crystal structure of human cathepsin K complexed with a potent inhibitor

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Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function

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The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme

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Location of the binding site for chloride ion activation of cathepsin C

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