| First Author | Lindfors HE | Year | 2011 |
| Journal | FEBS Lett | Volume | 585 |
| Issue | 4 | Pages | 601-5 |
| PubMed ID | 21266176 | Mgi Jnum | J:201301 |
| Mgi Id | MGI:5512946 | Doi | 10.1016/j.febslet.2011.01.026 |
| Citation | Lindfors HE, et al. (2011) Linker length dependent binding of a focal adhesion kinase derived peptide to the Src SH3-SH2 domains. FEBS Lett 585(4):601-5 |
| abstractText | 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. |
