NMR Dynamics-Derived Insights into the Binding Properties of a Peptide Interacting with an SH2 Domain

The signal transduction protein phospholipase C-γ1 (PLC-γ1) is activated when its C-terminal SH2 domain (PLCC) binds the phosphorylated Tyr-1021 site (pTyr-1021) in the β-platelet-derived growth factor receptor (PDGFR). To better understand the contributions that dynamics make to binding, we have us...

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Veröffentlicht in:	Biochemistry (Easton) 2005-01, Vol.44 (2), p.694-703
Hauptverfasser:	Finerty, Patrick J, Mittermaier, Anthony K, Muhandiram, Ranjith, Kay, Lewis E, Forman-Kay, Julie D
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides - chemistry Carbon Isotopes - chemistry Deuterium - chemistry Ligands Nanotechnology Nitrogen Isotopes - chemistry Nuclear Magnetic Resonance, Biomolecular - methods Oligopeptides - chemistry Oligopeptides - genetics Oligopeptides - metabolism Peptide Fragments - chemistry Peptide Fragments - metabolism Phospholipase C gamma Phosphotyrosine - genetics Phosphotyrosine - metabolism Platelet-Derived Growth Factor - genetics Protein Binding Protein Conformation Proto-Oncogene Proteins c-sis src Homology Domains Thermodynamics Time Factors Type C Phospholipases - chemistry Type C Phospholipases - metabolism
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