Figure 1.
(a) Surface representation of p150n with C traces
of ClipZn2 (pink) and p150n (green). Key interacting side chains
are shown as sticks (green atoms are sulfur). Blue, GKNDG motif;
orange, conserved hydrophobic residues (Phe52, Trp57 and Phe88;
Supplementary Fig. 3 online). Red circled region is expanded in
b. (b) Close-up views of interface between ClipZn2 and p150n.
Middle panel has same orientation as in a. Residues discussed in
the text are labeled. Orange sphere, water molecule mediating
the Arg90-Asn1422 interaction. (c) Pull-down assays of wild-type
and mutant ClipZn12 and p150n. p150n proteins were incubated
with glutathione S-transferase (GST)-fused ClipZn12 proteins.
Left lane contains wild-type p150n, for reference. Mock
pull-down is shown as a control (see Supplementary Table 2).
traces
of ClipZn2 (pink) and p150n (green). Key interacting side chains
are shown as sticks (green atoms are sulfur). Blue, GKNDG motif;
orange, conserved hydrophobic residues (Phe52, Trp57 and Phe88;
Supplementary Fig. 3 online). Red circled region is expanded in
b. (b) Close-up views of interface between ClipZn2 and p150n.
Middle panel has same orientation as in a. Residues discussed in
the text are labeled. Orange sphere, water molecule mediating
the Arg90-Asn1422 interaction. (c) Pull-down assays of wild-type
and mutant ClipZn12 and p150n. p150n proteins were incubated
with glutathione S-transferase (GST)-fused ClipZn12 proteins.
Left lane contains wild-type p150n, for reference. Mock
pull-down is shown as a control (see Supplementary Table 2).