Understanding the molecular basis of EGFR kinase domain/MIG-6 peptide recognition complex using computational analyses.

ABSTRACT:

Background

Epidermal growth factor receptor (EGFR) signalling plays a major role in biological processes, including cell proliferation, differentiation and survival. Since the over-expression of EGFR causes human cancers, EGFR is an attractive drug target. A tumor suppressor endogenous protein, MIG-6, is known to suppress EGFR over-expression by binding to the C-lobe of EGFR kinase. Thus, this C-lobe of the EGFR kinase is a potential new target for EGFR kinase activity inhibition. In this study, molecular dynamics (MD) simulations and binding free energy calculations were used to investigate the protein-peptide interactions between EGFR kinase and a 27-residue peptide derived from MIG-6_s1 segment (residues 336-362).

Results

These 27 residues of MIG-6_s1 were modeled from th

SUBMITTER: Moonrin N 

PROVIDER: S-EPMC4383062 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature