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Figure 4.
Structural models for interactions between SENP7 and SUMO. A,
superposition of the SENP7 and SENP2 catalytic domains in blue
ribbon and yellow stick representation, respectively. The
position of SUMO is indicated schematically based on the
position of SUMO2 in complex with SENP2 (PDB 2IO0). Several
residues within the SUMO-protease interface are highlighted in
stick representation and labeled according to their position and
side chain composition in SENP7. B, top panel, the structure of
SUMO2-RanGAP1 (stick and transparent surface representation) is
shown in complex with SENP2 (yellow ribbon representation) to
indicate the position of SUMO in site A (green) and the
substrate RanGAP1 in site B (pink). The bottom panel depicts the
SENP7 catalytic domain in a similar orientation to SENP2 in the
top panel to highlight the positions of Loop-2, Loop-3, and
Loop-4 with respect to the putative SUMO interaction surfaces in
site A, site B, and site C. C, close-up view of the interface
between SENP2 (yellow) and SUMO2 (green) with SENP7 (blue) shown
at the right in an analogous orientation to highlight residues
involved in interactions with SUMO at site A. D, similar to C,
but depicting the other side of the SENP2-SUMO2 complex to
highlight residues in SENP7 Loop-1 that may contribute to SUMO
interaction. E, electrostatic potential surface representation
for SENP1, SENP2, and SENP7 to highlight similarities between
SENP1 and SENP2 within the SUMO interaction surface (site A) and
the differences between SENP7 and either SENP1 or SENP2 in the
analogous surface. The relative position for SUMO in site A is
indicated by a green circle as derived from structures of
SENP1-SUMO, SENP2-SUMO and models for SENP7-SUMO.
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