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Models of the tertiary structures of cathepsins K, S, H, and F were constructed by using homology protein modelling methods and refinements by interactive graphics and energy minimisation. The predicted structures yield information regarding their substrate binding sites and indicate the residues surrounding these sites. The ligand binding sites were characterised and compared with each other by means of calculated molecular electrostatic surface potentials. This will allow designing and development of new ligands specific for these cathepsins in future investigations.
Development and validation of homology models of human cathepsins K, S, H, and F.,Fengler A, Brandt W Adv Exp Med Biol. 2000;477:255-60. PMID:10849752[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Fengler A, Brandt W. Development and validation of homology models of human cathepsins K, S, H, and F. Adv Exp Med Biol. 2000;477:255-60. PMID:10849752
