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13 June 2012 Characterization of EPPIN's Semenogelin I Binding Site: A Contraceptive Drug Target
Erick J.R. Silva, Katherine G. Hamil, Richard T. Richardson, Michael G. O'Rand
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Abstract

Epididymal protease inhibitor (EPPIN) is found on the surface of spermatozoa and works as a central hub for a sperm surface protein complex (EPPIN protein complex [EPC]) that inhibits sperm motility on the binding of semenogelin I (SEMG1) during ejaculation. Here, we identify EPPIN's amino acids involved in the interactions within the EPC and demonstrate that EPPIN's sequence C102-P133 contains the major binding site for SEMG1. Within the same region, the sequence F117-P133 binds the EPC-associated protein lactotransferrin (LTF). We show that residues Cys102, Tyr107, and Phe117 in the EPPIN C-terminus are required for SEMG1 binding. Additionally, residues Tyr107 and Phe117 are critically involved in the interaction between EPPIN and LTF. Our findings demonstrate that EPPIN is a key player in the protein-protein interactions within the EPC. Target identification is an important step toward the development of a novel male contraceptive, and the functionality of EPPIN's residues Cys102, Tyr107, and Phe117 offers novel opportunities for contraceptive compounds that inhibit sperm motility by targeting this region of the molecule.

Erick J.R. Silva, Katherine G. Hamil, Richard T. Richardson, and Michael G. O'Rand "Characterization of EPPIN's Semenogelin I Binding Site: A Contraceptive Drug Target," Biology of Reproduction 87(3), (13 June 2012). https://doi.org/10.1095/biolreprod.112.101832
Received: 2 May 2012; Accepted: 1 June 2012; Published: 13 June 2012
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