Homology modeling and molecular dynamics simulations of the glycine receptor ligand binding domain.

ABSTRACT: We present a homology based model of the ligand binding domain (LBD) of the homopentameric alpha1 glycine receptor (GlyR). The model is based on multiple sequence alignment with other members of the nicotinicoid ligand gated ion channel superfamily and two homologous acetylcholine binding proteins (AChBP) from the freshwater (Lymnaea stagnalis) and saltwater (Aplysia californica) snails with known high resolution structure. Using two template proteins with known structure to model three dimensional structure of a target protein is especially advantageous for sequences with low homology as in the case presented in this paper. The final model was cross-validated by critical evaluation of experimental and published mutagenesis, functional and other biochemical studies. In addition, a complex

SUBMITTER: Speranskiy K 

PROVIDER: S-EPMC2873197 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature