Figure 1.
Figure 1: Formation of the complex. Ribbon depictions of
native [1]-antitrypsin8
with trypsin aligned above it in the docking orientation (left),
and of the complex showing the 71 Å shift of the P1 methionine
of [1]-antitrypsin,
with full insertion of the cleaved reactive-centre loop into the
A-sheet (right). Regions of disordered structure in the
complexed trypsin are shown as interrupted coils projected from
the native structure of trypsin. Red, [1]-antitrypsin
-sheet
A; yellow, reactive-centre loop; green ball-and-stick, P1 Met;
cyan, trypsin (with helices in magenta for orientation); red
ball-and-stick, active serine 195.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2000,
407,
923-926)
copyright 2000.
[1]-antitrypsin8
with trypsin aligned above it in the docking orientation (left),
and of the complex showing the 71 Å shift of the P1 methionine
of 
-sheet
A; yellow, reactive-centre loop; green ball-and-stick, P1 Met;
cyan, trypsin (with helices in magenta for orientation); red
ball-and-stick, active serine 195.