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Figure 2.
Figure 2. Superimposition of the ICAM-3/HA Complex onto the
ICAM-5/dm-I Complex
ICAM-3/HA is in red and the ICAM-5/dm-I
complex is in cyan. For clarity, the ICAM-5 D2 is not shown in
the figures. The conserved Glu-37 is in yellow.
(A) The
superposition is based on I domains. Side chains at the two
mutation sites are shown in a ball-and-stick model with Phe265
and Phe292 in the HA replaced by Ser265 and Gly292 in the dm-I
domain, respectively. Also shown are Leu289s where the
polypeptide chains of the two I domains start to run opposite
directions.
(B) The ICAMs' domain D1s were used for
superposition. HA I domain from the ICAM-3/HA complex is not
shown for clarity. The loops of R41-T45 in ICAM-5 and S41-V45 in
ICAM-3 are colored green and magenta, respectively. Residue N43
and attached sugar NAG-2 from ICAM-5 D1 are also shown as a
ball-and-stick model.
(C) The stereo view of the local
region around MIDAS of superimposed I domains. The I domain from
ICAM-5 complex is in green, that from the ICAM-3 complex is in
cyan, and the closed form of the α[L] I domain (1ZOP) in
magenta. Glu-37 from ICAM-5 that binds to MIDAS is shown in
yellow. The metal ion is shown as a ball. Side chains of
residues D239, S265, F265, and G262 are labeled and shown in a
ball-and-stick model. The yellow arrows indicate the movement
direction of the β4α5 loop and the F265 ring from closed form
to open form.
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