2hv8: Difference between revisions

Revision as of 09:47, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hv8.png

Template:STRUCTURE 2hv8

Crystal structure of GTP-bound Rab11 in complex with FIP3Crystal structure of GTP-bound Rab11 in complex with FIP3

Template:ABSTRACT PUBMED 17007872

About this StructureAbout this Structure

2HV8 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes., Eathiraj S, Mishra A, Prekeris R, Lambright DG, J Mol Biol. 2006 Nov 24;364(2):121-35. Epub 2006 Aug 26. PMID:17007872

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OCA

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-[[Image:2hv8.gif|left|200px]]
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-'''Crystal structure of GTP-bound Rab11 in complex with FIP3'''
+===Crystal structure of GTP-bound Rab11 in complex with FIP3===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17007872}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17007872 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17007872}}
 ==About this Structure==
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 [[Category: Rab11a]]
 [[Category: Recycling endosome]]
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