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.
journal_name
BMC Bioljournal_title
BMC biologyauthors
Nussinov R,Ma Bdoi
10.1186/1741-7007-10-2subject
Has Abstractpub_date
2012-01-25 00:00:00pages
2issn
1741-7007pii
1741-7007-10-2journal_volume
10pub_type
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