The Src SH2 domain interacts dynamically with the focal adhesion kinase binding site as demonstrated by paramagnetic NMR spectroscopy

IUBMB Life

Volumn 64, Issue 6, 2012, Pages 538-544

  Lindfors, Hanna E ^a   Drijfhout, Jan Wouter ^b   Ubbink, Marcellus ^a  

^a LEIDEN UNIVERSITY   (Netherlands)

^b LEIDEN UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

calorimetry; dynamics; paramagnetic relaxation enhancement; peptide protein interaction; phosphopeptide; TOAC

Indexed keywords

FOCAL ADHESION KINASE; PROTEIN SH2;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; MICROCALORIMETRY; MOUSE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARAMAGNETIC RELAXATION ENHANCEMENT NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; ELECTRON SPIN RESONANCE SPECTROSCOPY; FOCAL ADHESION PROTEIN-TYROSINE KINASES; MICE; MOLECULAR SEQUENCE DATA; PHOSPHOPEPTIDES; PROTEIN BINDING; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES; SURFACE PROPERTIES; THERMODYNAMICS; TITRIMETRY;

EID: 84861328704     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1038     Document Type: Article

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