1br0

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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1br0 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1br0 ConSurf].
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== Publication Abstract from PubMed ==
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Syntaxin 1A plays a central role in neurotransmitter release through multiple protein-protein interactions. We have used NMR spectroscopy to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure. This 120-residue N-terminal domain is conserved in plasma membrane syntaxins but not in other syntaxins, indicating a specific role in exocytosis. The domain contains three long alpha helices that form an up-and-down bundle with a left-handed twist. A striking residue conservation is observed throughout a long groove that is likely to provide a specific surface for protein-protein interactions. A highly acidic region binds to the C2A domain of synaptotagmin I in a Ca2+-dependent interaction that may serve as an electrostatic switch in neurotransmitter release.
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Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.,Fernandez I, Ubach J, Dulubova I, Zhang X, Sudhof TC, Rizo J Cell. 1998 Sep 18;94(6):841-9. PMID:9753330<ref>PMID:9753330</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1br0" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Syntaxin 3D structures|Syntaxin 3D structures]]
*[[Syntaxin 3D structures|Syntaxin 3D structures]]
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

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THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A

PDB ID 1br0

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