3NUM

Substrate induced remodeling of the active site regulates HtrA1 activity

Summary for 3NUM

Entry DOI	10.2210/pdb3num/pdb
Related	3NWU
Descriptor	Serine protease HTRA1 (1 entity in total)
Functional Keywords	serine protease, degp, htra, protease, hydrolase
Biological source	Homo sapiens (human)
Cellular location	Secreted: Q92743
Total number of polymer chains	1
Total formula weight	36425.63
Authors	Truebestein, L.,Tennstaedt, A.,Hauske, P.,Krojer, T.,Kaiser, M.,Clausen, T.,Ehrmann, M. (deposition date: 2010-07-07, release date: 2011-02-23, Last modification date: 2023-09-06)
Primary citation	Truebestein, L.,Tennstaedt, A.,Monig, T.,Krojer, T.,Canellas, F.,Kaiser, M.,Clausen, T.,Ehrmann, M. Substrate-induced remodeling of the active site regulates human HTRA1 activity. Nat.Struct.Mol.Biol., 18:386-388, 2011 Cited by PubMed 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. PubMed: 21297635 DOI: 10.1038/nsmb.2013 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.75 Å)

Structure validation