Figure 2.
Figure 2: Comparison of hGBP1 and Ras structures. a,
Superimposition of the LG domain of hGBP1 with the G domain of
Ras in complex with GDP(PDB accession no. 1Q21) as a stereo
view. N-terminal residues 1-36 of hGBP1 up to 1
have been omitted for clarity. The colour code is as in Fig. 1;
Ras is in cyan. b, Putative location of nucleotide-binding site
in hGBP1. The regions of hGBP1 potentially involved in binding
the guanine nucleotide are shown as obtained from a structural
superimposition of RasGDP (in cyan) with the corresponding
regions in hGBP1 (purple), highlighting functionally important
residues necessary for binding and conformational change as
balls or in ball-and-stick. Whereas Gly 60^ras overlays very
well with Gly 100^hGBP1, residues D119/D184 and T35/T75 do not.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2000,
403,
567-571)
copyright 2000.
1
have been omitted for clarity. The colour code is as in Fig. 1;
Ras is in cyan. b, Putative location of nucleotide-binding site
in hGBP1. The regions of hGBP1 potentially involved in binding
the guanine nucleotide are shown as obtained from a structural
superimposition of RasGDP (in cyan) with the corresponding
regions in hGBP1 (purple), highlighting functionally important
residues necessary for binding and conformational change as
balls or in ball-and-stick. Whereas Gly 60^ras overlays very
well with Gly 100^hGBP1, residues D119/D184 and T35/T75 do not.