Figure 3.
Fig. 3. (A) Structural alignment of a model of the
single-chain, precursor form of the serine proteinase homology
domain of HGFl/MSP (green) and the crystal structure of the
corresponding two-chain form (pink). The model of the single
chain form of the protein was constructed with MODELLER[39],
using the atomic coordinates of the plasminogen -chain (pdb:
1QRZ) [24] as template. Residues discussed in the text are
labeled and shown as solid sticks. The figure was generated with
PYMOL [36]. (B) and (C) Surface representation of the serine
proteinase domains of two-chain HGFl/MSP (b) and the model of
single-chain HGFl/MSP (c). The amino acids shown in colour are
either those corresponding to the catalytic triad (on the left)
or amino acids in L13 that have been shown by mutagenesis to be
involved in receptor binding. The figure has been prepared with
SPOCK (http://quorum.tamu.edu/Manual/).
The above figure is reprinted
by permission from the Federation of European Biochemical Societies:
FEBS J
(2005,
272,
5799-5807)
copyright 2005.
-chain (pdb:
1QRZ) [24] as template. Residues discussed in the text are
labeled and shown as solid sticks. The figure was generated with
PYMOL [36]. (B) and (C) Surface representation of the serine
proteinase domains of two-chain HGFl/MSP (b) and the model of
single-chain HGFl/MSP (c). The amino acids shown in colour are
either those corresponding to the catalytic triad (on the left)
or amino acids in L13 that have been shown by mutagenesis to be
involved in receptor binding. The figure has been prepared with
SPOCK (http://quorum.tamu.edu/Manual/).