Peer-Reviewed Journal Details
Mandatory Fields
Jagoe, WN;Lindsay, AJ;Read, RJ;Mccoy, AJ;McCaffrey, MW;Khan, AR
2006
August
Structure
Crystal structure of Rab11 in complex with Rab11 family interacting protein 2
Validated
WOS: 63 ()
Optional Fields
RAB11-INTERACTING PROTEINS RECYCLING ENDOSOMES COUPLING PROTEIN EFFECTOR PROTEIN PLASMA-MEMBRANE TERMINAL DOMAIN MYOSIN VB BINDING IDENTIFICATION COMPARTMENT
14
1273
1283
The small GTPase Rab11 regulates the recycling of endosomes to the plasma membrane via interactions with the Rab11 family of interacting proteins (FIPs). FIPs contain a highly conserved Rab binding domain (RBD) at their C termini whose structure is unknown. Here, we have determined the crystal structure of the RBD of FIP2 in complex with Rab11(GTP) by single wavelength anomalous diffraction methods. The overall structure is a heterotetramer with dyad symmetry, arranged as a Rab11-(FIP2)(2)-Rab11 complex. FIP2 forms a central alpha-helical coiled coil, with both helices contributing to the Rab11 binding patch on equivalent and opposite sides of the homodimer. Switch 1 of Rab11 is embedded between the two helices, while switch 2 remains flexible and is peripherally associated with the effector. The complex reveals the structural basis for Rab11 recognition by Flips and suggests the molecular mechanisms underlying endocytic recycling pathways.
CAMBRIDGE
0969-2126
10.1016/j.str.2006.06.010
Grant Details