Figure 2.
Fig. 2. Panel a, backbone positions of the A loop and
C helix for
BTK-KD (green), phospho-LCK (red), and c-SRC (white) are
superimposed to illustrate their conformational differences and
similarities. An AMP-PNP molecule ( pink) is present in the
c-SRC crystal structure and was used to mark the location of
active site. The side chains of Arg-544 and Tyr-551 in BTK and
their equivalent residues in LCK and c-SRC on the A loop are
shown. All coordinates were superimposed in CHAIN (28). Prepared
using Insight II. Panel b, the noninhibitory (BTK) and
inhibitory (IRK) conformations of the A loop are illustrated.
Both crystal structures were first superimposed and shown
separately in the same orientation with the A loops highlighted
in rainbow tubes. Neither of the activation tyrosines is
phosphorylated in the crystal structures. Prepared with GRASP
(56).
C helix for
BTK-KD (green), phospho-LCK (red), and c-SRC (white) are
superimposed to illustrate their conformational differences and
similarities. An AMP-PNP molecule ( pink) is present in the
c-SRC crystal structure and was used to mark the location of
active site. The side chains of Arg-544 and Tyr-551 in BTK and
their equivalent residues in LCK and c-SRC on the A loop are
shown. All coordinates were superimposed in CHAIN (28). Prepared
using Insight II. Panel b, the noninhibitory (BTK) and
inhibitory (IRK) conformations of the A loop are illustrated.
Both crystal structures were first superimposed and shown
separately in the same orientation with the A loops highlighted
in rainbow tubes. Neither of the activation tyrosines is
phosphorylated in the crystal structures. Prepared with GRASP
(56).