2cjs: Difference between revisions
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[[Image:2cjs.gif|left|200px]] | [[Image:2cjs.gif|left|200px]] | ||
'''STRUCTURAL BASIS FOR A MUNC13-1 HOMODIMER- MUNC13-1- RIM HETERODIMER SWITCH: C2-DOMAINS AS VERSATILE PROTEIN-PROTEIN INTERACTION MODULES''' | {{Structure | ||
|PDB= 2cjs |SIZE=350|CAPTION= <scene name='initialview01'>2cjs</scene>, resolution 1.78Å | |||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURAL BASIS FOR A MUNC13-1 HOMODIMER- MUNC13-1- RIM HETERODIMER SWITCH: C2-DOMAINS AS VERSATILE PROTEIN-PROTEIN INTERACTION MODULES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2CJS is a [ | 2CJS is a [[Protein complex]] structure of sequences 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=2CJS OCA]. | ||
==Reference== | ==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:[http:// | 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: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: c2 | [[Category: c2 domain]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: exocytosis]] | [[Category: exocytosis]] | ||
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[[Category: neurotransmitter transport]] | [[Category: neurotransmitter transport]] | ||
[[Category: phorbol-ester binding]] | [[Category: phorbol-ester binding]] | ||
[[Category: protein-protein | [[Category: protein-protein interaction]] | ||
[[Category: rim]] | [[Category: rim]] | ||
[[Category: synapse]] | [[Category: synapse]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:17 2008'' | ||
Revision as of 14:16, 20 March 2008
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| 2cjs, resolution 1.78Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | ZN, EDO and GOL | ||||||||||||
| 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
2CJS is a Protein complex structure of sequences 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
Page seeded by OCA on Thu Mar 20 16:16:17 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Protein complex
- Rattus norvegicus
- Dai, H.
- Dulubova, I.
- Lu, J.
- Machius, M.
- Rizo, J.
- Sudhof, T C.
- Tomchick, D R.
- EDO
- GOL
- ZN
- Alternative splicing
- C2 domain
- Coiled coil
- Exocytosis
- Metal-binding
- Munc13
- Neurotransmitter release
- Neurotransmitter transport
- Phorbol-ester binding
- Protein-protein interaction
- Rim
- Synapse
- Synaptosome
- Transport
- Zinc
- Zinc finger