Figure 1.
Fig. 1. (A) Ribbon diagram of the -chain of
HGFl/MSP. The three residues replacing the catalytic triad of
active proteinases: Q522 (c57), Q568 (c102) and Y661 (c195) are
shown as solid sticks. Also shown are the five intradomain
disulfide bonds while a sixth disulfide connecting the - and -chains
[Cys468-Cys588 (c122)] is not shown in the figure. L4, L5, L8,
10, L11 and L13 define loops discussed in the text and detailed
in Fig. 2A. (B) Detailed view of the active site region of the
-chain of
HGFl/MSP. The three residues corresponding to the catalytic ones
of actives serine proteinases are shown in red; residues
corresponding to the S1 specificity pocket (L11) are shown in
blue; a segment of the L13 loop is shown in yellow. The
disulfide bond between C657 and C685 (c191-c220) is also shown.
The figure was generated with PYMOL[36] and 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 of
HGFl/MSP. The three residues replacing the catalytic triad of
active proteinases: Q522 (c57), Q568 (c102) and Y661 (c195) are
shown as solid sticks. Also shown are the five intradomain
disulfide bonds while a sixth disulfide connecting the 
- and