Parvin: Difference between revisions

<Structure load='Complex_parvin.pdb' size='360' scene='Alpha-parvin/Parvin/2' frame='true' align='left' caption='C-terminal CH domain of alpha-parvin bound to paxillin LD motif'/>

The <scene name='Alpha-parvin/Parvin/2'>scene on the left</scene> shows the superimposition of three structures of alpha-parvin bound to paxillin LD motifs, LD1 ([[2vzd]]), LD2 ([2vzg]] and LD4 ([[2vzi]]) respectively. These three LD motifs differ in sequence, but they are all helical. Surprisingly, the orientation of LD1 binding is reversed compared to that of LD2 and LD4. One of the LD motifs (LD1) is shown in the scene, represented by a blue helix. LD2 and LD4 bind in the same location. As you can see, all three peptides, despite different sequences and different binding orientations, induce a very similar conformation of alpha-parvin, as represented by a very good alignment of the three structures. In particular, residues 248 to 264, which experience conformational change upon binding, are similar in all complexes with RMSD values of 0.28 Å (LD1 versus LD2), 0.23 Å (LD1 versus LD4), and 0.15 Å (LD2 versus LD4) in 16 equivalent C^α positions.