Work

Protein dynamics and conformational selection in bidirectional signal transduction

Year: 2012

Type: article

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.

Source: BMC Biology

DOI: 10.1186/1741-7007-10-2

Authors: Ruth Nussinov, Buyong Ma

Institutions: Tel Aviv University, National Cancer Institute, Center for Cancer Research

Language: English

Topic: Axon Guidance and Neuronal Signaling

Subfield: Cellular and Molecular Neuroscience

Field: Neuroscience

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,690

Funders: U.S. Department of Health and Human Services, National Institutes of Health, U.S. Public Health Service, National Cancer Institute