Structure of human cathepsin D: comparison of inhibitor binding and subdomain displacement with other aspartic proteases.

Erickson, J W; Baldwin, E T; Bhat, T N; Gulnik, S

Erickson, J W; Baldwin, E T; Bhat, T N; Gulnik, S.

Affiliation

Erickson JW; Structural Biochemistry Program, PRI/DynCorp, NCI-Frederick Cancer Research and Development Center, Maryland 21702, USA.

Adv Exp Med Biol ; 362: 181-92, 1995.

Article in En | MEDLINE | ID: mdl-8540317

Subject(s)

Aspartic Acid Endopeptidases/chemistry; Cathepsin D/chemistry; Protein Structure, Secondary; Amino Acid Sequence; Animals; Aspartic Acid Endopeptidases/antagonists & inhibitors; Aspartic Acid Endopeptidases/metabolism; Binding Sites; Binding, Competitive; Cathepsin D/antagonists & inhibitors; Cathepsin D/isolation & purification; Crystallization; Crystallography, X-Ray; Humans; Hydrogen Bonding; Liver/enzymology; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Sequence Homology, Amino Acid; Swine

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Collection: 01-internacional Database: MEDLINE Main subject: Aspartic Acid Endopeptidases / Cathepsin D / Protein Structure, Secondary Limits: Animals / Humans Language: En Journal: Adv Exp Med Biol Year: 1995 Document type: Article

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