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Figure 2.
Fig. 2. The complex between GAP-334 and Ras. (A) Ribbon
representation of the complex model drawn with Molscript (52)
and^ Raster3D (53) according to the assignment of secondary
structure^ elements obtained with the program DSSP (54). The
extra and^ catalytic domains of GAP-334 are shown in green and
red (respectively), regions of GAP contacting Ras in light
brown, Ras in yellow, and^ GDP and AlF[3] as ball-and-stick
models. Regions involved in the^ interface are labeled, Sw I and
Sw II indicating the switch regions, C the COOH-terminal, and N
the NH[2]-terminal. (B) Schematic^ drawing with selected
interactions. Polar interactions between individual residues of
GAP-334 and Ras are shown as red lines for interactions of side
chains, and as red arrows for contacts from side chain to main
chain atoms, where the arrowhead marks the residue contributing
the main chain group. Yellow lines indicate^ van der Waals or
hydrophobic interactions. Some water molecules (marked W) from
the interface region are included. Residues belonging to the
interacting regions of Ras indicated in (A) are denoted^ with
specified boxes, as indicated. Interaction between Lys88 and
Thr791 is shown by a dashed arrow, because the electron density
in this region is presently not of sufficient quality to
unambiguously define the contact. Amino acid abbreviations are
in (55).
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