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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Bibliographische Detailangaben
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
Online-Zugang:	Volltext
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