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Figure 6.
FIG. 6. HGF  intermolecular contacts
and comparison to other proteins. A, intermolecular contacts in
HGF x-ray structure. The
reference molecule (green) has three crystal contacts. The blue
molecule arises from a 2-fold axis relating the N-terminal
regions Val496-Arg502 [c17-c23] and adjacent residues. The
N-terminal Val495 [c16] of the green and blue molecules are
depicted as spheres. The HGF -chain/ -chain
interface involving the N terminus and adjacent residues from
the [c140] and [c180] loops is shown by the arrow. The
salmon-colored molecule arises from a 2-fold axis relating
"active site regions." The side chains of Tyr673 [c195] are
shown. Residue C604S [c128] (sphere) in the yellow molecule
contacts the reference molecule in the [c70] loop. B, partial
sequences for HGF and homologous proteins at the border between
 -
and -chains. HGF and
chymotrypsinogen numbering are above and below sequences,
respectively. The boxed Cys in the -chain forms a
disulfide bond with a Cys in the -chain. t-PA, tissue
plasminogen activator.
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