Homology modeling, molecular docking, and molecular dynamics simulations elucidated α-fetoprotein binding modes.

ABSTRACT:

Background

An important mechanism of endocrine activity is chemicals entering target cells via transport proteins and then interacting with hormone receptors such as the estrogen receptor (ER). α-Fetoprotein (AFP) is a major transport protein in rodent serum that can bind and sequester estrogens, thus preventing entry to the target cell and where they could otherwise induce ER-mediated endocrine activity. Recently, we reported rat AFP binding affinities for a large set of structurally diverse chemicals, including 53 binders and 72 non-binders. However, the lack of three-dimensional (3D) structures of rat AFP hinders further understanding of the structural dependence for binding. Therefore, a 3D structure of rat AFP was built using homology modeling in order to elucidate rat AFP-lig

SUBMITTER: Shen J 

PROVIDER: S-EPMC3851483 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature