Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.febslet.2010.11.060
Title: An adjacent arginine, and the phosphorylated tyrosine in the c-Met receptor target sequence, dictates the orientation of c-Cbl binding
Authors: Sun, Q.
Ng, C.
Guy, G.R.
Sivaraman, J. 
Keywords: c-Casitas B-lineage lymphoma tyrosine kinase binding domain
Crystal structure
Hepatocyte growth factor receptor
Reverse binding
Surface plasmon resonance
Issue Date: 21-Jan-2011
Source: Sun, Q., Ng, C., Guy, G.R., Sivaraman, J. (2011-01-21). An adjacent arginine, and the phosphorylated tyrosine in the c-Met receptor target sequence, dictates the orientation of c-Cbl binding. FEBS Letters 585 (2) : 281-285. ScholarBank@NUS Repository. https://doi.org/10.1016/j.febslet.2010.11.060
Abstract: Previously, we have demonstrated that the tyrosine phosphorylated hepatocyte growth factor receptor (Met) binds to the c-Cbl phosphotyrosine- recognition, tyrosine kinase binding (TKB) domain in a reverse orientation compared to other c-Cbl binding partners. A Met peptide with the DpYR motif changed to RpYD (MetRD) retains a similar TKB binding affinity as the native Met peptide. However, the TKB: MetRD complex crystal structure reveals a complete reversal of the binding orientation. Collated data indicates that both binding and orientation is dictated by the phosphorylated tyrosine and an adjacent arginine forming intra-peptide hydrogen bonds and aligning unidirectionally with complementary charges in the phosphotyrosine binding pocket of c-Cbl. Structured summary: c-Cbl and MetRD bind: shown by x-ray crystallography (view interaction) c-Cbl and MetRD bind: shown by mass spectrometry studies of complexes (view interaction) c-Cbl bind to Met: shown by surface plasmon resonance (view interactions 1,2). © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Source Title: FEBS Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/100050
ISSN: 00145793
DOI: 10.1016/j.febslet.2010.11.060
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