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http://purl.uniprot.org/citations/17007872http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17007872http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17007872http://www.w3.org/2000/01/rdf-schema#comment"The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognize the active form of Rab11. Normal completion of cytokinesis requires a complex between Rab11 and FIP3. Here, we report the crystal structure and mutational analysis of a heterotetrameric complex between constitutively active Rab11 and a FIP3 construct that includes the RBD. Two Rab11 molecules bind to dyad symmetric sites at the C terminus of FIP3, which forms a non-canonical coiled-coiled dimer with a flared C terminus and hook region. The RBD overlaps with the coiled coil and extends through the C-terminal hook. Although FIP3 engages the switch and interswitch regions of Rab11, the mode of interaction differs significantly from that of other Rab-effector complexes. In particular, the switch II region undergoes a large structural rearrangement from an ordered but non-complementary active conformation to a remodeled conformation that facilitates the interaction with FIP3. Finally, we provide evidence that FIP3 can form homo-oligomers in cells, and that a critical determinant of Rab11 binding in vitro is necessary for FIP3 recruitment to recycling endosomes during cytokinesis."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.08.064"xsd:string
http://purl.uniprot.org/citations/17007872http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.08.064"xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/author"Lambright D.G."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/author"Lambright D.G."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/author"Mishra A."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/author"Mishra A."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/author"Prekeris R."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/author"Prekeris R."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/author"Eathiraj S."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/author"Eathiraj S."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/pages"121-135"xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/pages"121-135"xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/title"Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/title"Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes."xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/volume"364"xsd:string
http://purl.uniprot.org/citations/17007872http://purl.uniprot.org/core/volume"364"xsd:string
http://purl.uniprot.org/citations/17007872http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17007872
http://purl.uniprot.org/citations/17007872http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17007872