Figure 1.
Figure 1: Crystal structure of the apo-PPAR- bold gamma-.
a, Ribbons drawing of the apo-PPAR- LBD,
amino acids 207–476. The nomenclature of the helices is based
on the RXR- crystal
structure^16. -Helices
are light blue; -strands
are green; loops are brown. b, A worm backbone tracing of PPAR-
,
with a surface representation of the unoccupied van der Waals
space in the ligand-binding site. We determined the 'unoccupied'
volume by fitting in virtual atoms that did not occupy the van
der Waals surface of the protein. The total unoccupied volume is
1,300
Å^3. c, Sequence alignment of the human PPAR LBDs. Amino
acids that are conserved between PPARs ,
and
are
in yellow; the secondary structure that the sequence adopts in
PPAR- is
shown in red boxes for -helices
and blue arrows for -strands.
Residues involved in rosiglitazone binding are underlined. The
sequence alignment predicts that several residues involved in
direct interactions of PPAR- with
ligand are not conserved in the other PPAR subtypes, and
explains the specificity of TZDs for PPAR- :
residue H323 is not found in PPAR- ,
and Q286 is not found in PPAR- or
PPAR- .
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(1998,
395,
137-143)
copyright 1998.
.
a, Ribbons drawing of the apo-PPAR- 
LBD,
amino acids 207–476. The nomenclature of the helices is based
on the RXR- 
crystal
structure^16. 
-strands
are green; loops are brown. b, A worm backbone tracing of PPAR-
1,300
Å^3. c, Sequence alignment of the human PPAR LBDs. Amino
acids that are conserved between PPARs 
are
in yellow; the secondary structure that the sequence adopts in
PPAR-