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Updated: Feb 7, 2026
A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
Published on: November 2, 2018
Crystal structures of human procathepsin H
Yue Hao1,2, Whitney Purtha3, Christa Cortesio4
1Department of Molecular Engineering, Amgen Inc., Cambridge, MA, United States of America.
Abstract:
Cathepsin H is a member of the papain superfamily of lysosomal cysteine proteases. It is the only known aminopeptidase in the family and is reported to be involved in cancer and other major diseases. Like many other proteases, it is synthesized as an inactive proenzyme. Although the crystal structure of mature porcine cathepsin H revealed the binding of the mini-chain and provided structural basis for the aminopeptidase activity, detailed structural and functional information on the inhibition and activation of procathepsin H has been elusive. Here we present the crystal structures of human procathepsin H at 2.00 Å and 1.66 Å resolution. These structures allow us to explore in detail the molecular basis for the inhibition of the mature domain by the prodomain. Comparison with cathepsin H structure reveals how mini-chain reorients upon activation. We further demonstrate that procathepsin H is not auto-activated but can be trans-activated by cathepsin L.
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