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Figure 1.
Figure 1: Structure of the TRAF domain alone and in complex with
the TNF-R2 peptide. a, Stereo ribbon diagram of the TRAF
domain of human TRAF2 in the peptide-free structure. The  -strands,
 -helices
and loops are shown in cyan, yellow and purple, respectively.
The loop between 7
and 8
is highly flexible andexhibits a different conformation in the
peptide-bound structure b, Ribbon drawing of the trimeric TRAF
domain in complex with TNF-R2 peptide, looking down the
three-fold axis. The -strands
in each protomer are shown in cyan, green and dark blue. The
peptide is shown as a stick model for the protomer incyan.
Residues of the TRAF-C domain in the trimer interface (between
the protomers shown in cyan and dark blue) are also shown as
stick models. The TRAF-C domain of the structure obeys proper
three-fold symmetry, whereas the coiled-coil domain shows
significant deviations. c, As for b, except that the three-fold
axis is now vertical.
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