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. 2011 Mar;18(3):386-8.
doi: 10.1038/nsmb.2013. Epub 2011 Feb 6.

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

Linda Truebestein  1 , Annette Tennstaedt, Timon Mönig, Tobias Krojer, Flavia Canellas, Markus Kaiser, Tim Clausen, Michael Ehrmann
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Substrate-induced remodeling of the active site regulates human HTRA1 activity

Linda Truebestein et al. Nat Struct Mol Biol. 2011 Mar.

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.

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