title: 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.
authors.affiliation: Basic Research Program, SAIC-Frederick, Inc,, Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA. ruthnu@helix.nih.gov.
authors.forename: Ruth
authors.initials: R
authors.lastname: Nussinov
authors.forename: Buyong
authors.initials: B
authors.lastname: Ma