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Based on unique biology of prostate cancer, prostate‐specific antigen could be a useful target for prostate cancer therapies. Such targeting requires the identification of highly selective inhibitor‐binding sites. Three‐dimensional structure was calculated by homology modeling. The overall structure of human prostate‐specific antigen is composed of two β‐barrel domain, kallikrein loop and active‐site triad His⁵⁷, Asp¹⁰², and Ser¹⁹⁵. Structure of human prostate‐specific antigen is quite similar to hK‐1 and HPK‐3. The major differences were observed at kallikrein loop and position of active site. The substrate‐binding pocket is predominated by hydrophobic residues and the bottom of the specificity pocket contains Ser¹⁸⁹ as in chymotrypsin, which provides substrate specificity. The hydrophobic, and preferentially aromatic (Trp215), amino acid residues are determinant of substrate binding due to the presence of …