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2cjt

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[[Image:2cjt.gif|left|200px]]<br /><applet load="2cjt" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cjt.gif|left|200px]]<br /><applet load="2cjt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2cjt, resolution 1.44&Aring;" />
caption="2cjt, resolution 1.44&Aring;" />
'''STRUCTURAL BASIS FOR A MUNC13-1 HOMODIMER- MUNC13-1- RIM HETERODIMER SWITCH: C2-DOMAINS AS VERSATILE PROTEIN-PROTEIN INTERACTION MODULES'''<br />
'''STRUCTURAL BASIS FOR A MUNC13-1 HOMODIMER- MUNC13-1- RIM HETERODIMER SWITCH: C2-DOMAINS AS VERSATILE PROTEIN-PROTEIN INTERACTION MODULES'''<br />
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==About this Structure==
==About this Structure==
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2CJT 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 EDO and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Fmt Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CJT OCA].
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2CJT 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=EDO:'>EDO</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJT OCA].
==Reference==
==Reference==
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:25:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:36:12 2008''

Revision as of 08:36, 3 February 2008


2cjt, resolution 1.44Å

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STRUCTURAL BASIS FOR A MUNC13-1 HOMODIMER- MUNC13-1- RIM HETERODIMER SWITCH: C2-DOMAINS AS VERSATILE PROTEIN-PROTEIN INTERACTION MODULES

Overview

C(2) domains are well characterized as Ca(2+)/phospholipid-binding, modules, but little is known about how they mediate protein-protein, interactions. In neurons, a Munc13-1 C(2)A-domain/RIM zinc-finger domain, (ZF) heterodimer couples synaptic vesicle priming to presynaptic, plasticity. We now show that the Munc13-1 C(2)A domain homodimerizes, and, that homodimerization competes with Munc13-1/RIM heterodimerization. X-ray, diffraction studies guided by nuclear magnetic resonance (NMR) experiments, reveal the crystal structures of the Munc13-1 C(2)A-domain homodimer and, the Munc13-1 C(2)A-domain/RIM ZF heterodimer at 1.44 A and 1.78 A, resolution, respectively. The C(2)A domain adopts a beta-sandwich, structure with a four-stranded concave side that mediates, homodimerization, leading to the formation of an eight-stranded, beta-barrel. In contrast, heterodimerization involves the bottom tip of, the C(2)A-domain beta-sandwich and a C-terminal alpha-helical extension, which wrap around the RIM ZF domain. Our results describe the structural, basis for a Munc13-1 homodimer-Munc13-1/RIM heterodimer switch that may be, crucial for vesicle priming and presynaptic plasticity, uncovering at the, same time an unexpected versatility of C(2) domains as protein-protein, interaction modules, and illustrating the power of combining NMR, spectroscopy and X-ray crystallography to study protein complexes.

About this Structure

2CJT is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer switch., Lu J, Machius M, Dulubova I, Dai H, Sudhof TC, Tomchick DR, Rizo J, PLoS Biol. 2006 Jun;4(7):e192. PMID:16732694

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