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2a20
From Proteopedia
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[[Image:2a20.gif|left|200px]] | [[Image:2a20.gif|left|200px]] | ||
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'''Solution structure of Rim2 Zinc Finger Domain''' | '''Solution structure of Rim2 Zinc Finger Domain''' | ||
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[[Category: Schneggenburger, R.]] | [[Category: Schneggenburger, R.]] | ||
[[Category: Sudhof, T C.]] | [[Category: Sudhof, T C.]] | ||
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Revision as of 15:30, 3 May 2008
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. 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 Sat May 3 18:30:08 2008
