1y8f
From Proteopedia
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|PDB= 1y8f |SIZE=350|CAPTION= <scene name='initialview01'>1y8f</scene> | |PDB= 1y8f |SIZE=350|CAPTION= <scene name='initialview01'>1y8f</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MUNC13-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= MUNC13-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8f OCA], [http://www.ebi.ac.uk/pdbsum/1y8f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y8f RCSB]</span> | ||
}} | }} | ||
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[[Category: Rizo, J.]] | [[Category: Rizo, J.]] | ||
[[Category: Shen, N.]] | [[Category: Shen, N.]] | ||
| - | [[Category: ZN]] | ||
[[Category: c1-domain]] | [[Category: c1-domain]] | ||
[[Category: cysteine-rich domain]] | [[Category: cysteine-rich domain]] | ||
[[Category: zinc-binding domain]] | [[Category: zinc-binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:00:09 2008'' |
Revision as of 22:00, 30 March 2008
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| Ligands: | |||||||
| Gene: | MUNC13-1 (Rattus norvegicus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the munc13-1 C1-domain
Overview
Protein kinase C (PKC) isozymes and other receptors of diacylglycerol (DAG) bind to this widespread second messenger through their C(1) domains. These alternative DAG receptors include munc13-1, a large neuronal protein that is crucial for DAG-dependent augmentation of neurotransmitter release. Whereas the structures of several PKC C(1) domains have been determined and have been shown to require little conformational changes for ligand binding, it is unclear whether the C(1) domains from other DAG receptors contain specific structural features with key functional significance. To gain insight into this question, we have determined the three-dimensional structure in solution of the munc13-1 C(1) domain using NMR spectroscopy. The overall structure includes two beta-sheets, a short C-terminal alpha-helix, and two Zn(2+)-binding sites, resembling the structures of PKC C(1) domains. However, the munc13-1 C(1) domain exhibits striking structural differences with the PKC C(1) domains in the ligand-binding site. These differences result in occlusion of the binding site of the munc13-1 C(1) domain by a conserved tryptophan side chain that in PKCs adopts a completely different orientation. As a consequence, the munc13-1 C(1) domain requires a considerable conformational change for ligand binding. This structural distinction is expected to decrease the DAG affinity of munc13-1 compared to that of PKCs, and is likely to be critical for munc13-1 function. On the basis of these results, we propose that augmentation of neurotransmitter release may be activated at higher DAG levels than PKCs as a potential mechanism for uncoupling augmentation of release from the multitude of other signaling processes mediated by DAG.
About this Structure
1Y8F is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Intramolecular occlusion of the diacylglycerol-binding site in the C1 domain of munc13-1., Shen N, Guryev O, Rizo J, Biochemistry. 2005 Feb 1;44(4):1089-96. PMID:15667202
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