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. 2006 May 4;103(20):7637–7642. doi: 10.1073/pnas.0601638103

Fig. 3.

Fig. 3.

SOCS2 SH2 domain and binding of GHR phosphopeptide PVPDpYTSIHIV determined by ITC. (A) The SOCS2 substrate pocket has the common hydrophobic cluster at the +3 site, including L95 (βD6), L106 (βE4), Y129 (αB9), and L150 (BG3). The binding site of the phosphotyrosine moiety is indicated by the presence of a bound sulfate ion. Hydrogen bonds are shown as dotted lines. (B) Binding thermodynamic data determined by ITC showed that the GHR-derived phosphopeptide bound with an affinity of 1.6 μM.