2cjt

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[[Image:2cjt.gif|left|200px]]<br /><applet load="2cjt" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cjt.gif|left|200px]]
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caption="2cjt, resolution 1.44&Aring;" />
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'''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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{{Structure
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|PDB= 2cjt |SIZE=350|CAPTION= <scene name='initialview01'>2cjt</scene>, resolution 1.44&Aring;
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|SITE= <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURAL BASIS FOR A MUNC13-1 HOMODIMER- MUNC13-1- RIM HETERODIMER SWITCH: C2-DOMAINS AS VERSATILE PROTEIN-PROTEIN INTERACTION MODULES'''
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==Overview==
==Overview==
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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 <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].
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2CJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJT OCA].
==Reference==
==Reference==
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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 Jul;4(7):e192. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16732694 16732694]
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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 Jul;4(7):e192. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16732694 16732694]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: FMT]]
[[Category: FMT]]
[[Category: alternative splicing]]
[[Category: alternative splicing]]
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[[Category: c2 domains]]
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[[Category: c2 domain]]
[[Category: coiled coil]]
[[Category: coiled coil]]
[[Category: exocytosis]]
[[Category: exocytosis]]
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[[Category: neurotransmitter release]]
[[Category: neurotransmitter release]]
[[Category: phorbol-ester binding]]
[[Category: phorbol-ester binding]]
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[[Category: protein-protein interactions]]
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[[Category: protein-protein interaction]]
[[Category: rim]]
[[Category: rim]]
[[Category: synaptosome]]
[[Category: synaptosome]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:18 2008''

Revision as of 14:16, 20 March 2008

Image:2cjt.gif


PDB ID 2cjt

Drag the structure with the mouse to rotate
, resolution 1.44Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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. 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 Jul;4(7):e192. PMID:16732694

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