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BMC Biol. 2012 Jan 25;10:2. doi: 10.1186/1741-7007-10-2.

Protein dynamics and conformational selection in bidirectional signal transduction.

Author information

1
Basic Research Program, SAIC-Frederick, Inc,, Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA. ruthnu@helix.nih.gov.

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.

PMID:
22277130
PMCID:
PMC3266202
DOI:
10.1186/1741-7007-10-2
[Indexed for MEDLINE]
Free PMC Article
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