Figure 5.
(a) Crystal structure of chicken c-SRC-T338I bound to ATP
S.
SRC-T338I is homologous to T334I in human c-SRC. Chicken SRC
residues are numbered according to the human c-SRC kinase
numbering. The residues Leu328, Met317, Phe408 and His387, which
constitute the hydrophobic spine, are shown in blue. The
gatekeeper isoleucine residue is shown in orange. The activation
loop is shown in red. (b) The inactive conformation of chicken
c-SRC (PDB 2SRC), colored as in a. (c) Active site of Lck kinase
(PDB 1QPC) in the active state bound with AMP-PNP shown in
yellow. Gatekeeper residue Thr316 and the catalytic Lys273 are
shown as green surfaces. The water molecules sandwiched between
the residues Thr316 and Lys273 are shown as red circles. The
interactions of lysine with ANP and the catalytic Glu288 are
shown; bond distances are presented in angstroms. (d) Active
site of SRC-T341I kinase domain (PDB 3DQW) bound with ATP S
shown in yellow. The surfaces of the side chains for residues
Ile341 and Lys298 are shown in green. Interactions of Lys298
with Glu310 and ATP S
are mapped and the bond distances are indicated in angstroms.
(e) Active site of insulin receptor kinase (IRK; PDB entry 1GAG)
bound with ANP shown in yellow. The surfaces of the side chains
for residues Met1076 and Lys1030 are shown in green.
Interactions of catalytic Lys1030 with Glu1047 and ANP are
mapped, and the bond distances are indicated in angstroms.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
Nat Struct Biol
(2008,
15,
1109-1118)
copyright 2008.
S.
SRC-T338I is homologous to T334I in human c-SRC. Chicken SRC
residues are numbered according to the human c-SRC kinase
numbering. The residues Leu328, Met317, Phe408 and His387, which
constitute the hydrophobic spine, are shown in blue. The
gatekeeper isoleucine residue is shown in orange. The activation
loop is shown in red. (b) The inactive conformation of chicken
c-SRC (PDB 2SRC), colored as in a. (c) Active site of Lck kinase
(PDB 1QPC) in the active state bound with AMP-PNP shown in
yellow. Gatekeeper residue Thr316 and the catalytic Lys273 are
shown as green surfaces. The water molecules sandwiched between
the residues Thr316 and Lys273 are shown as red circles. The
interactions of lysine with ANP and the catalytic Glu288 are
shown; bond distances are presented in angstroms. (d) Active
site of SRC-T341I kinase domain (PDB 3DQW) bound with ATP