2q3x

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spinqualitylabelsall models 2q3x, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The RIM1alpha C2B domain

Overview

RIM proteins play critical roles in synaptic vesicle priming and diverse, forms of presynaptic plasticity. The C-terminal C2B domain is the only, module that is common to all RIMs but is only distantly related to, well-studied C2 domains, and its three-dimensional structure and, interactions have not been characterized in detail. Using NMR, spectroscopy, we now show that N- and C-terminal extensions beyond the, predicted C2B domain core sequence are necessary to form a folded, stable, RIM1alpha C2B domain. We also find that the isolated RIM1alpha C2B domain, is not sufficient for previously described protein-protein interactions, involving the RIM1alpha C-terminus, suggesting that additional sequences, adjacent to the C2B domain might be required for these interactions., However, analytical ultracentrifugation shows that the RIM1alpha C2B, domain forms weak dimers in solution. The crystal structure of the, RIM1alpha C2B domain dimer at 1.7 A resolution reveals that it forms a, beta-sandwich characteristic of C2 domains and that the unique N- and, C-terminal extensions form a small subdomain that packs against the, beta-sandwich and mediates dimerization. Our results provide a structural, basis to understand the function of RIM C2B domains and suggest that, dimerization may be a crucial aspect of RIM function.

About this Structure

2Q3X is a Single protein structure of sequence from Rattus norvegicus with SO4, NA and CL as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the RIM1alpha C2B domain at 1.7 A resolution., Guan R, Dai H, Tomchick DR, Dulubova I, Machius M, Sudhof TC, Rizo J, Biochemistry. 2007 Aug 7;46(31):8988-98. Epub 2007 Jul 14. PMID:17630786

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