Binding interactions of epididymal protease inhibitor and semenogelin-1: a homology modeling, docking and molecular dynamics simulation study.

ABSTRACT: Epididymal protease inhibitor (EPPIN) that is located on the sperm surface and specific to the male reproductive system is a non-hormonal contraceptive target, since the binding of EPPIN with the seminal plasma protein semenogelin-1 (SEMG1) causes a loss of sperm function. Here, we investigated the binding interactions between EPPIN and SEMG1 by homology modeling, docking and molecular dynamics simulation. Since no crystal structure was reported for EPPIN, its 3D structure was constructed by homology modeling and refined by dynamics simulation, illustrating the C-terminus domain of EPPIN could bind with its N-terminus domain through the residues 30-32 and 113-116. The binding interaction of SEMG1^10-8 peptide and EPPIN was investigated by Z-DOCK and dynamics simulation. After eva

SUBMITTER: Shan C 

PROVIDER: S-EPMC6686837 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature