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2a20
From Proteopedia
(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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| - | [[Image:2a20.gif|left|200px]]<br /><applet load="2a20" size=" | + | [[Image:2a20.gif|left|200px]]<br /><applet load="2a20" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2a20" /> | caption="2a20" /> | ||
'''Solution structure of Rim2 Zinc Finger Domain'''<br /> | '''Solution structure of Rim2 Zinc Finger Domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | alpha-RIMs and Munc13s are active zone proteins that control priming of | + | 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== | ==About this Structure== | ||
| - | 2A20 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2A20 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A20 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rizo, J.]] | [[Category: Rizo, J.]] | ||
[[Category: Schneggenburger, R.]] | [[Category: Schneggenburger, R.]] | ||
| - | [[Category: Sudhof, T | + | [[Category: Sudhof, T C.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: zinc-finger domain]] | [[Category: zinc-finger domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:47 2008'' |
Revision as of 14:22, 21 February 2008
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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 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 Thu Feb 21 16:22:47 2008
