Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR and MD simulations.

Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR and MD simulations.

The 16 EphA and EphB receptors represent the largest family of receptor tyrosine kinases, and their interactions with 9 ephrin-A and ephrin-B ligands initiate bidirectional signals controlling many physiological and pathological processes. Most interactions occur between receptor and ephrins of the...

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Bibliographic Details
Main Authors: Xuelu Huan, Jiahai Shi, Liangzhong Lim, Sayantan Mitra, Wanlong Zhu, Haina Qin, Elena B Pasquale, Jianxing Song
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3782497?pdf=render

Internet

http://europepmc.org/articles/PMC3782497?pdf=render

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