Interaction of the hub protein DYNLL with LC8 peptide

LC8 dynein light chain (DYNLL) is a hub protein, capable of binding proteins of various functions and influence their action. Being a dimeric protein with two equal binding sites it is thought to function as a dimerization engine. The structure of its complex with a high affinity binding peptide developed by in vitro evolutionary technique was determined by X-ray crystallography for characterizing specific interactions of the protein. In the complex the peptide was dimerized by a designed leuzine zipper in order to mimic the natural dimer binding to dimer mechanism and study possible distortion of the interactions in the dimer to dimer complex.

The structure of the DYNLL (grey) /  LC8 (colored by B-factor) complex

Cooperation

Motor Proteins: Structural Biology Research Group of the Department of Biochemistry, Eötvös Loránd University, Budapest
Directed Evolution Research Group of the Department of Biochemistry, Eötvös Loránd University, Budapest

Structure determined (PDB code): 

3P8M