1eea

Acetylcholinesterase

spinqualitylabelsall models 1eea, resolution 4.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1eea is a 1 chain structure with sequence from Electrophorus electricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Acetylcholinesterase, with EC number 3.1.1.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACES_TORCA] 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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acetylcholinesterase 3D structures

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