Fig. 2
From: Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase
Structures of the DH and PH domains by NMR and X-ray crystallography. a Bundle of 20 DH structures as determined by NMR spectroscopy. The long and flexible α4–α5 loop region (residues 622–638) is highlighted in red. b Cartoon representation of the NMR conformer closest to the mean. The six helical elements and the α4–α5 loop region are labeled. c Crystal structure of the DH domain in complex with Mb(Bcr-DH_4) in cartoon representation. The α4–α5 loop region is missing in this structure (black arrow). The monobody interacts with the DH domain via its FG loop, which is labeled. d Crystal structure of the internally deleted PH domain (PHΔ770–829) in complex with Mb(Bcr-PH_4) in cartoon representation. The monobody interacts with the PH domain via its FG loop, which is labeled. e Cartoon representation of the PH domain (PHΔ770–829) with assignment of the secondary structure elements, the internal deletion site covering residues 770–829 and the C-terminal linker region
