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Figure 4.
Fig. 4. Domain with cytokine activity. Stereo views of
EMAP II are shown as C  traces,
truncated at residue 133 for a clear view. The view is in the
same orientation as Fig. 3B. The domain, consisting of the
residues 13-57, which is homologous to the chemokines, is shown
in gray and consists of three strands (  1- 3) and one
short helix ( 1). The
peptide sequence (residues 12-18) involved in chemotaxis of EMAP
II is positioned at the beginning of this homologous domain.
Three residues, Cys-15, Ile-17, and Thr-18, which were exposed
to solvent, are shown by ball-and-stick symbols close to the end
of strand 1. The other
functional peptide sequence (residues 6-11) is located at the
other side of a loop formed by residues 99-102. The hydrophobic
residues Val-6, Leu-8, and Leu-11 form a shallow hydrophobic
pocket with Phe-107 and Leu-132. N represents the location of
Pro-3 and C the location of His-133. The C s of
residues 12, 99, and 102 are shown as black circles.
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