Schubert lab: bacterial InIC disrupts human Tuba complexes

[This figure is shown rotating on the right when first viewing the page. To see other figure click on the green links. To get back to this figure (in the original orientation), click on the Figure 1a green link above]

Spacefilling representation of the Tuba SH3-6 domain (green) binding to the human N-WASP peptide (red and red dots) and the Mena peptide (yellow). This is a superposition of two separate structures. The SH3 domain binds either peptide, but not at the same time. To see the red dots better, click on +/- quality at the bottom of the 3D browser window.

Detail of the interaction showing conserved and non-conserved residues of Tuba making contacts with the N-WASP peptide (red). You can make this figure less busy by turning off the labels (+/- labels switch on the bottom of the 3D browser). You can also look at it as a stereoview (right click under style>stereographic) after opening a pop-up window.

InIC Recognition of Tuba SH3-6, with the SH3-6 domain of Tuba in green, the Leucine Rich Repeat domain of InIC in purple and the remainder of InIC in blue. The (translucent) of the proteins takes a while to load but shows the tight contact of the interacting proteins.

Details of InIC/Tuba SH3-6 Interaction. F146 of InIC is crucial for the interaction - binding becomes about 100-times weaker when phenylalanine 146 is replaced by alanine (data not shown here, but in the original paper [[1]]). Back to the overall view of .

The SH3-6 domain of Tuba (green cartoon) binds both to InIC (cyan and purple cartoon) and to the N-WASP peptide (red spacefilling), but not at the same time. In the figure, the two complexes are superposed, and there are steric clashes (atoms bumping into each other) between InIC's leucine rich repeat (purple) and N-WASP (red). Thus, binding to those two binding partners is mutually exclusive.

Surface representation of the Tuba SH3-6 domain, with atoms that contact InIC in blue, atoms that contact N-WASP in pink, and atoms that contact both in the respective complex structures (remember, they can't bind at the same time) in gray. This figure is also available in a , which takes a while to load.

(bonus figure)

To give you an idea how superpositions work, here are the structures of Tuba-SH3 in complex with N-WASP (green and red) and Tuba-SH3 in complex with MENA (green and yellow). In this figure, the two complexes are far away from each other (they are based on two different experiments, we are just putting them into the same picture).

If you click on the "superpose" button below, jmol will overlay carbon alpha atoms of residues 1518-1573 of the SH3 domains as best as possible to minimize the distance between corresponding atoms. The SH3 domain has a slightly different conformation in the two structures, so the best is a superposition with an root mean square deviation (RMSD) of about 0.3 Ångström. The "separate" button will undo the superposition. Be sure to superpose the structures before you go back to other figures (like Fig 1a), otherwise they might look different.