Figure 1.
Figure 1. (a) Sequence alignment of PTP D1 domains of CRYP-2,
RPTP- and
RPTP- ,
and PTP1B. The secondary structure elements corresponding to
CRYP-2 are shown. A grey background has been used to highlight
residues involved in oligomerization. These are poorly
conserved. (b) The quaternary arrangement of CRYP-2 showing the
location of the two active sites. The active site of CRYP-2
(highlighted by the red circle) is not occluded by
oligomerization. The active site cysteine, aspartate, proline,
tryptophan, and the bound nitrate ion are depicted in ball and
stick representation. (c) Both open and closed conformations of
the active site lid are seen in the crystal structure. In this
superposition, the red ribbon representation is for CRYP-2 while
the superposed PTP1B conformation is seen in grey. (d and e) The
active site of CRYP-2 contains a nitrate ion in both the closed
and open conformations. Panels d (closed conformation) and e
(open conformation) show the (2Fo-Fc) electron density map
calculated at 1.2 for
the residues that surround the active site as well as the bound
nitrate ion.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2007,
68,
1011-1015)
copyright 2007.
and
RPTP- 
,
and PTP1B. The secondary structure elements corresponding to
CRYP-2 are shown. A grey background has been used to highlight
residues involved in oligomerization. These are poorly
conserved. (b) The quaternary arrangement of CRYP-2 showing the
location of the two active sites. The active site of CRYP-2
(highlighted by the red circle) is not occluded by
oligomerization. The active site cysteine, aspartate, proline,
tryptophan, and the bound nitrate ion are depicted in ball and
stick representation. (c) Both open and closed conformations of
the active site lid are seen in the crystal structure. In this
superposition, the red ribbon representation is for CRYP-2 while
the superposed PTP1B conformation is seen in grey. (d and e) The
active site of CRYP-2 contains a nitrate ion in both the closed
and open conformations. Panels d (closed conformation) and e
(open conformation) show the (2Fo-Fc) electron density map
calculated at 1.2 
for
the residues that surround the active site as well as the bound
nitrate ion.