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. 2013 Jun 11;11(6):e1001581. doi: 10.1371/journal.pbio.1001581

Figure 3. The hIKK2 dimer interface.

Figure 3

(A) Ribbon diagram (top) and space filling (bottom) representations of six hIKK2 protomers in the asymmetric unit. The individual subunit chains are labeled A–F and rainbow colored. (B) Ribbon diagrams of three hIKK2 dimers taken from the asymmetric unit. The distances between P578 residues from each hIKK2 in the dimers are labeled. For comparison, the xIKK2 crystal structure observed is shown below in its relatively closed conformation. (C) Overlay of the SDD from six monomers in the hIKK2 asymmetric unit. The three dimers overlay perfectly at their SDD distal ends (inside dashed box). Movement about a hinge point (black arrowheads) results in the differences observed in the portions of the SDD more proximal to the KD. (D) A close-up view reveals the series of hydrophobic and ionic interactions that mediate the dimer interface. (E) Superposition of the A:F dimer SDD from the hIKK2 structure and the xIKK2 dimer. (F) Close-up view of the boxed region from panel D reveals additional interactions present within the interface of the xIKK2 structure SDD. (G) In vitro kinase assays monitoring the activity of immunoprecipitated HA-IKK2 toward IκBα. Mutations targeting the dimer interface (lanes 3–5) are compared against the wild-type protein (lane 2).