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|Title: ||Ab initio structure of human seminal plasma prostatic inhibin gives significant insight into its biological functions|
|Authors: ||JOSHI, RR|
|Keywords: ||nonparametric regression|
|Issue Date: ||2002|
|Citation: ||JOURNAL OF MOLECULAR MODELING, 8(2), 50-57|
|Abstract: ||Human seminal plasma prostatic inhibin (HSPI) is a protein isolated from the human prostate gland. Despite its profound biomedical and biotechnological importance, the 3D structure of this protein of 94 amino acids remains undeciphered. The difficulties in extracting it in pure form and crystallizing it have restrained the determination of its structure experimentally. The homology- based computational methods are also not applicable, as HSPI lacks sufficient sequence homology with known structures in the protein data banks. We have predicted the structure of HSPI by a knowledge-based method using nonparametric multivariate statistical techniques. Stereochemical and other standard validation tests confirm this to be a well-refined structure. The biophysical properties exhibited by this structure are in good agreement with the NMR experimental observations. Docking and other computational studies on this structure provide significant explanation and insight into its binding activities and related biological and immunogenic functions and offer new directions for its potential applications.|
|Appears in Collections:||Article|
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