Structural thermodynamic study of the binding of renin inhibitors to endothiapepsin.
Gómez
J
J
Department of Biology and the Biocalorimetry Center, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Semo
N
N
Freire
E
E
D000808:Angiotensinogen / Q000031:analogs & derivatives / Q000378:metabolism; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D009842:Oligopeptides / Q000378:metabolism; D011480:Protease Inhibitors / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D000092502:Renin Inhibitors
D000808:Angiotensinogen; D016282:Aspartic Acid Endopeptidases; D009842:Oligopeptides; D011480:Protease Inhibitors; D000092502:Renin Inhibitors; C034503:H 77; C039583:H 142; C045142:H 189; C046598:H 261; C042466:Endothia aspartic proteinase