Protein dynamics and conformational selection in bidirectional signal transduction

Ruth Nussinov, Buyong Ma

Research output: Contribution to journalComment/debate

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.See research article http://www.biomedcentral.com/2046-1682/5/2.

Original languageEnglish
Article number2
JournalBMC Biology
Volume10
DOIs
StatePublished - 25 Jan 2012

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