2afx: Difference between revisions

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{{Seed}}
[[Image:2afx.png|left|200px]]


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==Crystal structure of human glutaminyl cyclase in complex with 1-benzylimidazole==
The line below this paragraph, containing "STRUCTURE_2afx", creates the "Structure Box" on the page.
<StructureSection load='2afx' size='340' side='right'caption='[[2afx]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2afx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AFX FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1BN:1-BENZYL-1H-IMIDAZOLE'>1BN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_2afx| PDB=2afx |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2afx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2afx OCA], [https://pdbe.org/2afx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2afx RCSB], [https://www.ebi.ac.uk/pdbsum/2afx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2afx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/2afx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2afx ConSurf].
<div style="clear:both"></div>


===Crystal structure of human glutaminyl cyclase in complex with 1-benzylimidazole===
==See Also==
 
*[[Glutaminyl cyclase|Glutaminyl cyclase]]
 
== References ==
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{{ABSTRACT_PUBMED_16135565}}
 
==About this Structure==
2AFX is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AFX OCA].
 
==Reference==
<ref group="xtra">PMID:16135565</ref><references group="xtra"/>
[[Category: Glutaminyl-peptide cyclotransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Cheng, W J.]]
[[Category: Large Structures]]
[[Category: Huang, K F.]]
[[Category: Cheng WJ]]
[[Category: Ko, T P.]]
[[Category: Huang KF]]
[[Category: Liu, Y L.]]
[[Category: Ko TP]]
[[Category: Wang, A H.J.]]
[[Category: Liu YL]]
[[Category: Alpha-beta protein]]
[[Category: Wang AHJ]]
[[Category: Metalloprotein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:25:33 2009''

Latest revision as of 16:41, 13 March 2024

Crystal structure of human glutaminyl cyclase in complex with 1-benzylimidazoleCrystal structure of human glutaminyl cyclase in complex with 1-benzylimidazole

Structural highlights

2afx is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.64Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

QPCT_HUMAN Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Schilling S, Hoffmann T, Manhart S, Hoffmann M, Demuth HU. Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions. FEBS Lett. 2004 Apr 9;563(1-3):191-6. PMID:15063747 doi:http://dx.doi.org/10.1016/S0014-5793(04)00300-X
  2. ↑ Cynis H, Rahfeld JU, Stephan A, Kehlen A, Koch B, Wermann M, Demuth HU, Schilling S. Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery. J Mol Biol. 2008 Jun 20;379(5):966-80. doi: 10.1016/j.jmb.2008.03.078. Epub 2008 , Apr 15. PMID:18486145 doi:http://dx.doi.org/10.1016/j.jmb.2008.03.078
  3. ↑ Huang KF, Liaw SS, Huang WL, Chia CY, Lo YC, Chen YL, Wang AH. Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding. J Biol Chem. 2011 Apr 8;286(14):12439-49. Epub 2011 Feb 1. PMID:21288892 doi:10.1074/jbc.M110.208595

2afx, resolution 1.64Å

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OCA
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