Crystal structure of human cathepsin K complexed with a potent inhibitor

Crystal structure of human cathepsin K complexed with a potent inhibitor

The high resolution structure of the new therapeutic target, cathepsin K, complexed with the potent mechanism-based inhibitor, APC3328, reveals the substrate-binding sites of this cysteine proteinase and validates the binding mode for this inhibitor class.

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Veröffentlicht in:Nature Structural Biology 1997-02, Vol.4 (2), p.105-109
Hauptverfasser: McGrath, Mary E, Klaus, Jeffrey L, Barnes, Michael G, Brömme, Dieter
Format: Artikel
Sprache:eng
Schlagworte:
Binding Sites
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Cathepsin K
Cathepsins - chemistry
Cathepsins - metabolism
correspondence
Crystallography, X-Ray
Cysteine Proteinase Inhibitors - chemistry
Cysteine Proteinase Inhibitors - pharmacology
Humans
Life Sciences
Membrane Biology
Models, Molecular
Molecular Conformation
Piperazines - chemistry
Piperazines - pharmacology
Protein Structure
Protein Structure, Secondary
Software
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Beschreibung
Zusammenfassung:The high resolution structure of the new therapeutic target, cathepsin K, complexed with the potent mechanism-based inhibitor, APC3328, reveals the substrate-binding sites of this cysteine proteinase and validates the binding mode for this inhibitor class.
ISSN:1072-8368
2331-365X
1545-9985
DOI:10.1038/nsb0297-105