Protein dynamics and conformational selection in bidirectional signal transduction.

ABSTRACT: Protein conformational dynamics simultaneously allow promiscuity and specificity in binding. The multiple conformations of the free EphA4 ligand-binding domain observed in two new EphA4 crystal structures provide a unique insight into the conformational dynamics of EphA4 and its signaling pathways. The heterogeneous ensemble and loop dynamics explain how the EphA4 receptor is able to bind multiple A- and B-ephrin ligands and small molecules via conformational selection, which helps to fine-tune cellular signal response in both receptor and ligand cells.

SUBMITTER: Nussinov R 

PROVIDER: S-EPMC3266202 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature