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Crystal structure of human osteoclast cathepsin K complex with E-64. 1997

B Zhao, and C A Janson, and B Y Amegadzie, and K D'Alessio, and C Griffin, and C R Hanning, and C Jones, and J Kurdyla, and M McQueney, and X Qiu, and W W Smith, and S S Abdel-Meguid

UI MeSH Term Description Entries
D007930 Leucine An essential branched-chain amino acid important for hemoglobin formation. L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008968 Molecular Conformation The characteristic three-dimensional shape of a molecule. Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D010010 Osteoclasts A large multinuclear cell associated with the BONE RESORPTION. An odontoclast, also called cementoclast, is cytomorphologically the same as an osteoclast and is involved in CEMENTUM resorption. Odontoclasts,Cementoclast,Cementoclasts,Odontoclast,Osteoclast
D002403 Cathepsins A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES. Cathepsin
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D015853 Cysteine Proteinase Inhibitors Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES. Acid Cysteine Proteinase Inhibitor,Cysteine Protease Inhibitor,Cysteine Protease Inhibitors,Cysteine Proteinase Antagonist,Cysteine Proteinase Antagonists,Cysteine Proteinase Inhibitor,Cysteine Proteinase Inhibitors, Endogenous,Cysteine Proteinase Inhibitors, Exogenous,alpha-Cysteine Protease Inhibitor,Acid Cysteine Proteinase Inhibitors,alpha-Cysteine Protease Inhibitors,Antagonist, Cysteine Proteinase,Antagonists, Cysteine Proteinase,Inhibitor, Cysteine Protease,Inhibitor, Cysteine Proteinase,Inhibitor, alpha-Cysteine Protease,Inhibitors, Cysteine Protease,Inhibitors, Cysteine Proteinase,Inhibitors, alpha-Cysteine Protease,Protease Inhibitor, Cysteine,Protease Inhibitor, alpha-Cysteine,Protease Inhibitors, Cysteine,Protease Inhibitors, alpha-Cysteine,Proteinase Antagonist, Cysteine,Proteinase Antagonists, Cysteine,Proteinase Inhibitor, Cysteine,Proteinase Inhibitors, Cysteine,alpha Cysteine Protease Inhibitor,alpha Cysteine Protease Inhibitors
D017433 Protein Structure, Secondary The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D056657 Cathepsin K A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.

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