1joc

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Revision as of 15:36, 12 November 2007

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spinqualitylabelsall models 1joc, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

EEA1 homodimer of C-terminal FYVE domain bound to inositol 1,3-diphosphate

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Early endosome autoantigen localization to early endosomes is mediated by, a C-terminal region, which includes a calmodulin binding motif, a Rab5, interaction site, and a FYVE domain that selectively binds phosphatidyl, inositol 3-phosphate. The crystal structure of the C-terminal region bound, to inositol 1,3-bisphosphate reveals an organized, quaternary assembly, consisting of a parallel coiled coil and a dyad-symmetric FYVE domain, homodimer. Structural and biochemical observations support a multivalent, mechanism for endosomal localization in which domain organization, dimerization, and quaternary structure amplify the weak affinity and, modest specificity of head group interactions with conserved residues. A, unique mode of membrane engagement deduced from the quaternary structure, of the C-terminal region provides insight into the structural basis of, endosome tethering.

Disease

Known disease associated with this structure: Spastic paraplegia 33 OMIM:[610243]

About this Structure

1JOC is a Single protein structure of sequence from Homo sapiens with ZN and ITP as ligands. The following page contains interesting information on the relation of 1JOC with [Zinc Fingers]. Full crystallographic information is available from OCA.

Reference

Multivalent endosome targeting by homodimeric EEA1., Dumas JJ, Merithew E, Sudharshan E, Rajamani D, Hayes S, Lawe D, Corvera S, Lambright DG, Mol Cell. 2001 Nov;8(5):947-58. PMID:11741531

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