Thermodynamics and proton uptake for pepstatin binding to retroviral and eukaryotic aspartic proteases.
Xie
D
D
Structural Biochemistry Program, SAIC Frederick, National Cancer Institute, Frederick Cancer Research and Development Center, Maryland 21702-1201, USA.
Gulnik
S
S
Collins
L
L
Gustchina
E
E
Bhat
T N
TN
Erickson
J W
JW
D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000201:enzymology; D016333:HIV Protease / Q000378:metabolism*; D017320:HIV Protease Inhibitors / Q000378:metabolism*; D006801:Humans; D010436:Pepstatins / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism*; D011522:Protons; D013816:Thermodynamics
D017320:HIV Protease Inhibitors; D010436:Pepstatins; D011480:Protease Inhibitors; D011522:Protons; C014195:Streptomyces pepsin inhibitor; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C031375:pepstatin