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Figure 4.
Fig. 4. Three-dimensional structure of hMIP-1  D26A and
comparative positions of amino acid residues in hMIP-1 , hMIP-1
 , and RANTES
. A, stereo view of the overlay of the monomer backbone
structures of hMIP-1 D26A and
hMIP-1 . The
regions 1-15, 31-38, and 67-69, which are discussed in the text,
are shown as a thin trace, whereas the rest of the backbone is
shown as a thick trace. B, from left to right, space-filling
representations of the three-dimensional NMR structures of
hMIP-1 D26A,
RANTES (6), and hMIP-1 (5) are
shown to illustrate the relative positions of the key acidic
amino acid residues involved in chemokine self-association at
positions 26 and 66 (27 and 67 in hMIP-1 ) shaded in
dark gray. The positions of the basic residues in the 44, 45,
and 47 positions (positions 45, 46, and 47 in hMIP-1 ), which we
speculate may be involved in charge interactions leading to
self-association are shaded in light gray. The terminal residues
1-15 and 67-69 are not shown in this figure.
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