Structure of human cathepsin D: comparison of inhibitor binding and subdomain displacement with other aspartic proteases.
Structural Biochemistry Program, PRI/DynCorp, NCI-Frederick Cancer Research and Development Center, Maryland 21702, USA.
J W
JW
Erickson
E T
ET
Baldwin
T N
TN
Bhat
S
S
Gulnik
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D001667:Binding, Competitive; D002402:Cathepsin D / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D006860:Hydrogen Bonding; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013552:Swine
D046911:Macromolecular Substances; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D