1eea
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Electrophorus_electricus Electrophorus electricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EEA FirstGlance]. <br> | <table><tr><td colspan='2'>[[1eea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Electrophorus_electricus Electrophorus electricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EEA FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.5Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eea OCA], [https://pdbe.org/1eea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eea RCSB], [https://www.ebi.ac.uk/pdbsum/1eea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eea ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eea OCA], [https://pdbe.org/1eea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eea RCSB], [https://www.ebi.ac.uk/pdbsum/1eea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eea ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ACES_TETCF ACES_TETCF] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1eea 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=1eea ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cholinesterases occur in a family of molecular forms, both as homo-oligomers of catalytic subunits, which can be either soluble, amphiphilic or lipid-anchored to the membrane; and hetero-oligomers of catalytic subunits and structural subunits. The structural subunits afford a method for precise localization of cholinesterases for specific function. A number of mutagenesis studies suggest that the C-terminal region of one alternatively spliced form of cholinesterase is involved in association of catalytic subunits into tetramers and in the association of these tetramers with structural subunits, however, there is currently no structural information about this region. In addition, none of the mutagenesis studies have clearly defined the residues important in these interactions. Here, multiple sequence alignment, structure prediction techniques and analysis of three-dimensional structural data are combined with a re-examination of mutagenesis and biochemical data. Three-dimensional models for the C-terminal region and for soluble tetrameric cholinesterase are proposed, and a set of rules governing subunit association are formulated. The simple model for association of catalytic and structural subunits presented is consistent with data for all known cholinesterases from species as divergent as nematode and man. | ||
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| - | Interactions underlying subunit association in cholinesterases.,Giles K Protein Eng. 1997 Jun;10(6):677-85. doi: 10.1093/protein/10.6.677. PMID:9278281<ref>PMID:9278281</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1eea" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] | *[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Acetylcholinesterase]] | ||
[[Category: Electrophorus electricus]] | [[Category: Electrophorus electricus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Giles | + | [[Category: Giles K]] |
| - | [[Category: Howard | + | [[Category: Howard AJ]] |
| - | [[Category: Phillips | + | [[Category: Phillips Jr GN]] |
| - | [[Category: Raves | + | [[Category: Raves ML]] |
| - | [[Category: Schmid | + | [[Category: Schmid MF]] |
| - | [[Category: Schrag | + | [[Category: Schrag JD]] |
| - | [[Category: Silman | + | [[Category: Silman I]] |
| - | [[Category: Sussman | + | [[Category: Sussman JL]] |
| - | [[Category: Wah | + | [[Category: Wah C]] |
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Revision as of 05:58, 9 August 2023
Acetylcholinesterase
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