Figure 5
![Figure 5](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2F1756-0500-3-14/MediaObjects/13104_2009_Article_418_Fig5_HTML.jpg)
Hypothesis generated on basis an in silico interaction of c-Kit (PDB: 1pgk) and Shp-2 (2shp). N-sh2 domain of Shp-1 recognizes the dual-phosphorylated tyrosines at juxtamembrane (Y568V569Y570) by PY pocket. Shp-1 forms a stable complex with c-Kit kinase by making intermolecular H-bonds with Lys818 and Asn819, using Tyr 100 and Ser28 of N-sh2 domain, following disruption of the intramolecular hydrogen bonding of Asp816 with Lys818 and Asn819 in activated c-Kit.