Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 3, Pages 386-388Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2013
Keywords
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Funding
- Deutsche Forschungsgemeinschaft
- Austrian Science Fund (FWF) [I 235] Funding Source: researchfish
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Crystal structures of active and inactive conformations of the human serine protease HTRA1 reveal that substrate binding to the active site is sufficient to stimulate proteolytic activity. HTRA1 attaches to liposomes, digests misfolded proteins into defined fragments and undergoes substrate-mediated oligomer conversion. In contrast to those of other serine proteases, the PDZ domain of HTRA1 is dispensable for activation or lipid attachment, indicative of different underlying mechanistic features.
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