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Figure 2.
MIDAS of the I domain in different conformations. The MIDAS
residues of the I domain are shown as stick models and colored
with purple carbon atoms in IA in the AL-57/IA structure (A),
green carbon atoms in HA in the ICAM-3/HA structure (B, PDB code
1T0P) and cyan carbon atoms in the unligated IA with closed
conformation (C, PDB code 1MJN). Acidic residues from ligands
D101 in AL-57 (A) and E37 in ICAM-3 (B), are also shown as stick
models with yellow carbon atoms. All oxygen atoms are in red.
Metal ions in the MIDAS are labeled and shown as spheres. Waters
in MIDAS are shown as red spheres and labeled with a “w.”
Coordination bonds are shown as dashed lines. Compared to the
closed conformation in the unligated IA, in which D239
coordinated to the MIDAS metal ion directly (C), D239 in IA(A)
or HA (B) coordinated to the metal ion via a water molecule and
the metal ion shifted about 2.3Å and coordinated to T206
directly.
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