Crystal structures of human procathepsin H

Hao, Yue; Purtha, Whitney; Cortesio, Christa; Rui, Huan; Gu, Yan; Chen, Hao; Sickmier, E. Allen; Manzanillo, Paolo; Huang, Xin

doi:10.1371/journal.pone.0200374

Crystal structures of human procathepsin H

Journal Article · Wed Jul 25 00:00:00 EDT 2018 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0200374· OSTI ID:1506499

Hao, Yue ^[1]; Purtha, Whitney ^[2]; Cortesio, Christa ^[2]; Rui, Huan ^[1]; Gu, Yan ^[1]; Chen, Hao ^[1]; Sickmier, E. Allen ^[1]; Manzanillo, Paolo ^[2]; ^[1]

Amgen Inc., Cambridge, MA (United States)
Amgen Inc., South San Francisco, CA (United States)

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.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: Amgen Discovery Research

OSTI ID:: 1506499

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 7 Vol. 13; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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A simple purification procedure of buffalo lung cathepsin H, its properties and influence of buffer constituents on the enzyme activity Singh, Shalini; Sharma, Samir; Agarwal, Sudhir K. Biochemistry and Biophysics Reports, Vol. 22 https://doi.org/10.1016/j.bbrep.2020.100739	journal	July 2020
‘Patchiness’ and basic cancer research: unravelling the proteases Soond, Surinder M.; Kozhevnikova, Maria V.; Zamyatnin Jr, Andrey A. Cell Cycle, Vol. 18, Issue 15 https://doi.org/10.1080/15384101.2019.1632639	journal	June 2019

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