Warning: The NCBI web site requires JavaScript to function. more...
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.See research article http://www.biomedcentral.com/2046-1682/5/2.
Images from this publication.See all images (2) Free text
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on