@article{46679f195a974e6aa4267a9d699eee8d,
title = "Protein dynamics and conformational selection in bidirectional signal transduction",
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.",
author = "Ruth Nussinov and Buyong Ma",
note = "Funding Information: The authors are funded in whole or in part with Federal funds from the National Cancer Institute, National Institutes of Health, under contract number HHSN261200800001E. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products, or organizations imply endorsement by the US Government. This research was supported (in part) by the Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research.",
year = "2012",
month = jan,
day = "25",
doi = "10.1186/1741-7007-10-2",
language = "אנגלית",
volume = "10",
journal = "BMC Biology",
issn = "1741-7007",
publisher = "BioMed Central Ltd.",
}