Figure 1.
Figure 1. Structure of D1 protease. a, Ribbon drawing of D1P.
The A domain is in red, the B domain in yellow and the C domain
in blue. The extended -hairpin
loop from the C domain forms an integral part of the folding
domain A and is regarded as part of that domain. The loops that
connect domains A to B and B to C have very high temperature
factors and are colored in green. The side chains of the
residues involved in catalysis or substrate binding, K397, S372
and R247, are shown in ball-and-stick representation. The GVGL
loop in the B domain, highlighted in magenta, has been shown to
be involved in the binding of the C-terminal residues of the
peptide ligand in the structurally homologous third PDZ domain
of synaptic protein PSD-95^25. b, Stereo view of the C trace
of D1P. Every 10^th residue and the N-terminus and C-terminus
are labeled. The disulfide bond between Cys 260 and Cys 451 is
shown in yellow. The orientation of the molecule is the same as
the standard orientation in (a).
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2000,
7,
749-753)
copyright 2000.
-hairpin
loop from the C domain forms an integral part of the folding
domain A and is regarded as part of that domain. The loops that
connect domains A to B and B to C have very high temperature
factors and are colored in green. The side chains of the
residues involved in catalysis or substrate binding, K397, S372
and R247, are shown in ball-and-stick representation. The GVGL
loop in the B domain, highlighted in magenta, has been shown to
be involved in the binding of the C-terminal residues of the
peptide ligand in the structurally homologous third PDZ domain
of synaptic protein PSD-95^25. b, Stereo view of the C 
trace
of D1P. Every 10^th residue and the N-terminus and C-terminus
are labeled. The disulfide bond between Cys 260 and Cys 451 is
shown in yellow. The orientation of the molecule is the same as
the standard orientation in (a).