Related Experiment Video
Updated: Jun 5, 2026

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
Published on: September 28, 2018
Linker length dependent binding of a focal adhesion kinase derived peptide to the Src SH3-SH2 domains
Hanna E Lindfors1, Bharat Somireddy Venkata, Jan W Drijfhout
1Leiden University, Leiden Institute of Chemistry, Leiden, The Netherlands.
Abstract:
The interaction between a peptide encompassing the SH3 and SH2 binding motifs of focal adhesion kinase (FAK) and the Src SH3-SH2 domains has been investigated with NMR spectroscopy and calorimetry. The binding to both motifs is anti-cooperative. Reduction of the long linker connecting the motifs does not lead to cooperativity. Short linkers that do not allow simultaneous intramolecular binding of the peptide to both motifs cause peptide-mediated dimerisation, even with a linker of only three amino acids. The role of the SH3 binding motif is discussed in view of the independent nature of the SH interactions.
Related Concept Videos
Intracellular Signaling Affects Focal Adhesions
Some...
Ligand Binding and Linkage
Ligand Binding and Linkage
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Cytoskeletal Linker Proteins - Plakins
Receptor Tyrosine Kinases
