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| | {{STRUCTURE_1y8f| PDB=1y8f | SCENE= }} | | {{STRUCTURE_1y8f| PDB=1y8f | SCENE= }} |
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| - | '''Solution structure of the munc13-1 C1-domain'''
| + | ===Solution structure of the munc13-1 C1-domain=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15667202}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15667202 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15667202}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1Y8F 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=1Y8F OCA]. | + | 1Y8F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y8F OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[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 Sat May 3 16:00:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:21:13 2008'' |
Revision as of 04:21, 28 July 2008
Template:STRUCTURE 1y8f
Solution structure of the munc13-1 C1-domain
Template:ABSTRACT PUBMED 15667202
About this Structure
1Y8F is a Single protein structure of sequence from Rattus norvegicus. Full experimental 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
Page seeded by OCA on Mon Jul 28 07:21:13 2008
