An adjacent arginine, and the phosphorylated tyrosine in the c-Met receptor target sequence, dictates the orientation of c-Cbl binding

Autor: Graeme R. Guy, Cherlyn Ng, J. Sivaraman, Qingxiang Sun
Rok vydání: 2010
Předmět:
Phosphotyrosine binding
Arginine
Reverse binding
Amino Acid Motifs
Biophysics
Peptide
macromolecular substances
Crystallography
X-Ray
Biochemistry
environment and public health
Mass Spectrometry
Structural Biology
hemic and lymphatic diseases
Genetics
Humans
Receptors
Growth Factor
Epidermal growth factor receptor
Amino Acid Sequence
Proto-Oncogene Proteins c-cbl
Tyrosine
Phosphotyrosine
Molecular Biology
chemistry.chemical_classification
biology
Hydrogen bond
Hepatocyte growth factor receptor
Crystal structure
c-Casitas B-lineage lymphoma tyrosine kinase binding domain
Hydrogen Bonding
Cell Biology
Proto-Oncogene Proteins c-met
Surface Plasmon Resonance
enzymes and coenzymes (carbohydrates)
Kinetics
chemistry
Hepatocyte Growth Factor Receptor
biology.protein
Phosphorylation
Protein Binding
Zdroj: FEBS letters. 585(2)
ISSN: 1873-3468
Popis: 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 summaryc-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)
Databáze: OpenAIRE
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