Figure 2.
Figure 2 Ribbon representation of one tryptase monomer in the
standard orientation. Monomer A of Fig. 1a is shown after
rotation around a vertical axis by 90°
(the rotation used to create Fig. 1b). The view is towards the
active centre (represented by Ser 195, His 57 and Asp 102 as
yellow stick models), with the active-site cleft running from
left to right; the APPA molecule interacts with Asp 189 (yellow
stick models) in the S1 pocket. The six unique surface loops of
tryptase surrounding the active site and engaged in intermonomer
contacts are specifically coloured. The 147 loop is light blue;
the 70-80 loop is yellow; the 37 loop is orange; the 60 loop is
mauve; the 97 loop is green; and the 173 flap is red. All other
tryptase segments are violet. Figure produced with Insight II
(Biosym/MSI, San Diego).
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(1998,
392,
306-311)
copyright 1998.
90°
(the rotation used to create Fig. 1b). The view is towards the
active centre (represented by Ser 195, His 57 and Asp 102 as
yellow stick models), with the active-site cleft running from
left to right; the APPA molecule interacts with Asp 189 (yellow
stick models) in the S1 pocket. The six unique surface loops of
tryptase surrounding the active site and engaged in intermonomer
contacts are specifically coloured. The 147 loop is light blue;
the 70-80 loop is yellow; the 37 loop is orange; the 60 loop is
mauve; the 97 loop is green; and the 173 flap is red. All other
tryptase segments are violet. Figure produced with Insight II
(Biosym/MSI, San Diego).