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2a20
From Proteopedia
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(New page: 200px<br /><applet load="2a20" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a20" /> '''Solution structure of Rim2 Zinc Finger Domai...)
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Revision as of 05:45, 21 November 2007
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Solution structure of Rim2 Zinc Finger Domain
Overview
alpha-RIMs and Munc13s are active zone proteins that control priming of, synaptic vesicles to a readily releasable state, and interact with each, other via their N-terminal sequences. The alpha-RIM N-terminal sequence, also binds to Rab3s (small synaptic vesicle GTPases), an interaction that, regulates presynaptic plasticity. We now demonstrate that alpha-RIMs, contain adjacent but separate Munc13- and Rab3-binding sites, allowing, formation of a tripartite Rab3/RIM/Munc13 complex. Munc13 binding is, mediated by the alpha-RIM zinc-finger domain. Elucidation of the, three-dimensional structure of this domain by NMR spectroscopy facilitated, the design of a mutation that abolishes alpha-RIM/Munc13 binding., Selective disruption of this interaction in the calyx of Held synapse, decreased the size of the readily releasable vesicle pool. Our data, suggest that the ternary Rab3/RIM/Munc13 interaction approximates synaptic, vesicles to the priming machinery, providing a substrate for presynaptic, plasticity. The modular architecture of alpha-RIMs, with nested binding, sites for Rab3 and other targets, may be a general feature of Rab, effectors that share homology with the alpha-RIM N-terminal sequence.
About this Structure
2A20 is a Single protein structure of sequence from Rattus norvegicus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?, Dulubova I, Lou X, Lu J, Huryeva I, Alam A, Schneggenburger R, Sudhof TC, Rizo J, EMBO J. 2005 Aug 17;24(16):2839-50. Epub 2005 Jul 28. PMID:16052212
Page seeded by OCA on Wed Nov 21 07:52:26 2007
