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Updated: Aug 7, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
Published on: September 30, 2016
Purification, crystallization and preliminary X-ray diffraction studies of Rab11 in complex with Rab11-FIP2
William N Jagoe1, Sarah R Jackson, Andrew J Lindsay
1School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland.
Abstract:
The small GTPase Rab11 regulates the recycling of endosomes back to the plasma membrane. In its active GTP-bound form, Rab11 binds a novel set of effectors termed the Rab11 family of interacting proteins (Rab11-FIPs) which contain a conserved C-terminal Rab-binding domain (RBD) of unknown structure. Here, a complex of Rab11 with the RBD of Rab11-FIP2 has been purified and crystallized in the trigonal space group P3(1)21, with unit-cell parameters a = 64.99, b = 64.99, c = 112.59 angstroms. Static light-scattering analyses of the molecular weight of the complex in solution are consistent with two copies of Rab11 and two copies of Rab11-FIP2 in the complex.
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