2d3g

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Revision as of 19:19, 12 November 2007

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spinqualitylabelsall models 2d3g, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Double sided ubiquitin binding of Hrs-UIM

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Hrs has an essential role in sorting of monoubiquitinated receptors to, multivesicular bodies for lysosomal degradation, through recognition of, ubiquitinated receptors by its ubiquitin-interacting motif (UIM). Here, we, present the structure of a complex of Hrs-UIM and ubiquitin at 1.7-A, resolution. Hrs-UIM forms a single alpha-helix, which binds two ubiquitin, molecules, one on either side. These two ubiquitin molecules are related, by pseudo two-fold screw symmetry along the helical axis of the UIM, corresponding to a shift by two residues on the UIM helix. Both ubiquitin, molecules interact with the UIM in the same manner, using the Ile44, surface, with equal binding affinities. Mutational experiments show that, both binding sites of Hrs-UIM are required for efficient degradative, protein sorting. Hrs-UIM belongs to a new subclass of double-sided UIMs, in contrast to its yeast homolog Vps27p, which has two tandem single-sided, UIMs.

Disease

Known disease associated with this structure: Sanfilippo syndrome, type C OMIM:[610453]

About this Structure

2D3G is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting., Hirano S, Kawasaki M, Ura H, Kato R, Raiborg C, Stenmark H, Wakatsuki S, Nat Struct Mol Biol. 2006 Mar;13(3):272-7. Epub 2006 Feb 5. PMID:16462748

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