Structure of Prostasin in Complex with Aprotinin

Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations.

UNP residues 45-305, Peptidase S1 domain

Serine protease 8, Prostasin light chain, Prostasin heavy chain

Basic protease inhibitor, BPTI, BPI, Aprotinin

ITGGSSAVAGQWPWQVSITYEGVHVCGGSLVSEQWVLSAAHCFPSEHHKEAYEVKLGAHQLDSYSEDAKVSTLKDIIPHP
SYLQEGSQGDIALLQLSRPITFSRYIRPISLPAAQASFPNGLHCTVTGWGHVAPSVSLLTPKPLQQLEVPLISRETCNSL
YNIDAKPEEPHFVQEDMVCAGYVEGGKDACQGDSGGPLSCPVEGLWYLTGIVSWGDACGARNRPGVYTLASSYASWIQSK
VTELQPRVVPQTQESQPDSNL

1.6M potassium hydrogen phosphate,
0.4M sodium dihydrogen phosphate, 0.2M sodium
chloride in an imidazole buffer at pH 8.0., VAPOR DIFFUSION, SITTING DROP, temperature 293K

Prostasin, hCAP1, channel Activating, Aprotinin, inhibition, Disulfide bond, Pharmaceutical, Protease inhibitor, Secreted, Serine protease inhibitor, Cell membrane, Glycoprotein, Hydrolase, Membrane, Protease, Serine protease, Transmembrane, Zymogen, HYDROLASE-INHIBITOR COMPLEX

ITGGSSAVAGQWPWQVSITYEGVHVCGGSLVSEQWVLSAAHCFPSEHHKEAYEVKLGAHQLDSYSEDAKVSTLKDIIPHP
SYLQEGSQGDIALLQLSRPITFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLLTPKPLQQLEVPLISRETCNCL
YNIDAKPEEPHFVQEDMVCAGYVEGGKDACQGDSGGPLSCPVEGLWYLTGIVSWGDACGARNRPGVYTLASSYASWIQSK
VTELQPRVVPQTQESQPDSNL