High quality structure of cleaved PAI-1-stab.
Here we report the crystal structure of a stablilized plasminogen activator inhibitor-1 variant (PAI-1-N150H-K154T-Q301P-Q319L-M354I (PAI-1-stab)) that shows a cleavage within the reactive centre loop. The new structure is of superior quality compared to the previously determined structure of the cleaved PAI-1-A335P mutant. We present a detailed comparison of the two structures and also compare them with the structure of the active PAI-1-stab. The structural data give important insights into the working mechanism of PAI-1 and also explain the role of various stabilizing mutations.
Dewilde
M
M
Katholieke Universiteit Leuven, Belgium.
Strelkov
S V
SV
Rabijns
A
A
Declerck
P J
PJ
D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D009154:Mutation; D017395:Plasminogen Activator Inhibitor 1 / Q000235:genetics* / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D015843:Serpins / Q000737:chemistry
D017395:Plasminogen Activator Inhibitor 1; D015843:Serpins