User:Markus Wiederstein/Sandbox 1: Difference between revisions

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==Your Heading Here (maybe something like 'Structure')== 2
==Crystal Structure of Human Acetylcholinesterase==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='4pqe' size='340' side='right' caption='[[4pqe]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
This is a default text for your page '''Markus Wiederstein/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
== Structural highlights ==
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
<table><tr><td colspan='2'>[[4pqe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PQE FirstGlance]. <br>
 
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lii|3lii]], [[4ey4|4ey4]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqe RCSB], [http://www.ebi.ac.uk/pdbsum/4pqe PDBsum]</span></td></tr>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref> 
== Structural relationships in TopSearch ==
[https://topsearch.services.came.sbg.ac.at/?code=1crn&query=1crn&pdbitem=bio Biological assemblies]


== Disease ==
[https://topsearch.services.came.sbg.ac.at/?code=1crn&query=1crn&pdbitem=chn Chains]
 
== Relevance ==
 
== Structural highlights ==
 
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


</StructureSection>
[https://topsearch.services.came.sbg.ac.at/?code=1crn&query=1crn&pdbitem=asu Asymmetric units]
== References ==
== References ==
<references/>
<references/>
__TOC__
</StructureSection>

Revision as of 12:11, 2 December 2016

Crystal Structure of Human AcetylcholinesteraseCrystal Structure of Human Acetylcholinesterase

Structural highlights

4pqe is a 1 chain structure. 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, RCSB, PDBsum

Function

[ACES_HUMAN] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.[1] [2] [3] [4]

Structural relationships in TopSearch

Biological assemblies

Chains

Asymmetric units

References

  1. ↑ Chhajlani V, Derr D, Earles B, Schmell E, August T. Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 1989 Apr 24;247(2):279-82. PMID:2714437
  2. ↑ Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A. The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. J Biol Chem. 1991 Dec 15;266(35):23977-84. PMID:1748670
  3. ↑ Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al.. Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem. 1992 Sep 5;267(25):17640-8. PMID:1517212
  4. ↑ Yang L, He HY, Zhang XJ. Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells. Neurosci Res. 2002 Apr;42(4):261-8. PMID:11985878

4pqe, resolution 2.90Å

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