The adaptor protein paxillin contains five conserved leucine-rich (LD) motifs that interact with a variety of focal adhesion proteins, such as alpha-parvin. Here, we report the first crystal structure of the C-terminal calponin homology domain (CH(C)) of alpha-parvin at 1.05 A resolution and show that it is able to bind all the LD motifs, with some selectivity for LD1, LD2, and LD4. Cocrystal structures with these LD motifs reveal the molecular details of their interactions with a common bind...Expand abstract
- Publication status:
- Publisher copy:
- Copyright date:
Structural analysis of the interactions between paxillin LD motifs and alpha-parvin.
If you are the owner of this record, you can report an update to it here: Report update to this record