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Purification, crystallization and preliminary X-ray diffraction studies of Rab11 in complex with Rab11-FIP2.

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.

SUBMITTER: Jagoe WN 

PROVIDER: S-EPMC2242937 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction studies of Rab11 in complex with Rab11-FIP2.

Jagoe William N WN   Jackson Sarah R SR   Lindsay Andrew J AJ   McCaffrey Mary W MW   Khan Amir R AR  

Acta crystallographica. Section F, Structural biology and crystallization communications 20060626 Pt 7

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. Stati  ...[more]

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