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Crystal structure of the Rab-binding domain of Rab11 family-interacting protein 2.

Aoife Mairead KearneyAmir Rafiq Khan
Published in: Acta crystallographica. Section F, Structural biology communications (2020)
The small GTPases Rab11, Rab14 and Rab25 regulate membrane trafficking through the recruitment of Rab11 family-interacting proteins (FIPs) to endocytic compartments. FIPs are multi-domain effector proteins that have a highly conserved Rab-binding domain (RBD) at their C-termini. Several structures of complexes of Rab11 with RBDs have previously been determined, including those of Rab11-FIP2 and Rab11-FIP3. In addition, the structures of the Rab14-FIP1 and Rab25-FIP2 complexes have been determined. All of the RBD structures contain a central parallel coiled coil in the RBD that binds to the switch 1 and switch 2 regions of the Rab. Here, the crystal structure of the uncomplexed RBD of FIP2 is presented at 2.3 Å resolution. The structure reveals antiparallel α-helices that associate through polar interactions. These include a remarkable stack of arginine residues within a four-helix bundle in the crystal lattice.
Keyphrases
  • immune response
  • dendritic cells
  • mass spectrometry
  • binding protein
  • dna binding
  • amino acid
  • type iii