High‐resolution structural analysis shows how different crystallographic environments can induce alternative modes of binding of a phosphotyrosine peptide to the SH2 domain of Fer tyrosine kinase

Fes and Fes‐related (Fer) protein tyrosine kinases (PTKs) comprise a subfamily of nonreceptor tyrosine kinases characterized by a unique multidomain structure composed of an N‐terminal Fer/CIP4 homology‐Bin/Amphiphysin/Rvs (F‐BAR) domain, a central Src homology 2 (SH2) domain, and a C‐terminal PTK d...

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Veröffentlicht in:	Protein science 2019-11, Vol.28 (11), p.2011-2019
1. Verfasser:	Matsuura, Yoshiyuki
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding sites Crystal structure Crystallography Crystallography, X-Ray Domains Fer Homology Humans Kinases ligand recognition Models, Molecular Peptides - chemistry phosphorylation Phosphotyrosine Phosphotyrosine - chemistry Protein Binding Protein Conformation Protein structure Protein Structure Reports Protein-tyrosine kinase Protein-Tyrosine Kinases - chemistry Protein-Tyrosine Kinases - metabolism SH2 domain src Homology Domains Structural analysis Tyrosine tyrosine kinase
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