Substrate-induced remodeling of the active site regulates human HTRA1 activity

Truebestein, Linda, Tennstaedt, Annette, Mönig, Timon, Krojer, Tobias, Canellas, Flavia, Kaiser, Markus, Clausen, Tim and Ehrmann, Michael ORCID: https://orcid.org/0000-0002-1927-260X 2011. Substrate-induced remodeling of the active site regulates human HTRA1 activity. Nature Structural & Molecular Biology 18 (3) , pp. 386-388. 10.1038/nsmb.2013

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Abstract

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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Subjects:	Q Science > QH Natural history > QH426 Genetics
Publisher:	Nature Publishing Group
ISSN:	1545-9993
Last Modified:	24 Oct 2022 10:44
URI:	https://orca.cardiff.ac.uk/id/eprint/45669

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