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BMC Biol. 2012; 10: 2.
Published online Jan 25, 2012. doi:  10.1186/1741-7007-10-2
PMCID: PMC3266202
Protein dynamics and conformational selection in bidirectional signal transduction
Ruth Nussinovcorresponding author1,2 and Buyong Ma1
1Basic Research Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA
2Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel
corresponding authorCorresponding author.
Ruth Nussinov: ruthnu/at/helix.nih.gov; Buyong Ma: mabuyong/at/mail.nih.gov
Received January 9, 2012; Accepted January 25, 2012.
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.
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