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Figure 1.
Fig. 1. The structure of melanoma inhibitory activity
protein.  -strands are
in blue, regions lacking regular secondary structure are in
green, 3[10] helices are in red, and disulfide bonds are in
gold. (A) View of the two sheets that
pack at right angles to each other. Sheet I is in front. 1 and 7 add onto
sheet II of the SH3 -sandwich.
The top of the barrel is toward the top of the page. (B) View
looking into one end (mouth) of the barrel. The 30s-40s loop
(analogous to the RT loop of SH3 domains) and the 60s-70s loop,
flank one mouth of the barrel. The N-terminal residues preceding
1 and the
C-terminal residues following 7 run along
the outside face of sheet II. A and B are on the same scale.
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