Leiden University, Leiden Institute of Chemistry, Leiden, The Netherlands.
FEBS Lett. 2011 Feb 18;585(4):601-5. doi: 10.1016/j.febslet.2011.01.026. Epub 2011 Jan 23.
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.
已经通过 NMR 光谱和量热法研究了包含粘着斑激酶（FAK）的 SH3 和 SH2 结合基序的肽与Src SH3-SH2 结构域之间的相互作用。与这两个基序的结合都是反协同的。连接基序的长接头的减少不会导致协同作用。不允许肽同时与两个基序进行分子内结合的短接头导致肽介导的二聚化，即使接头只有三个氨基酸。考虑到 SH 相互作用的独立性，讨论了 SH3 结合基序的作用。
