2zj4: Difference between revisions

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{{Seed}}
[[Image:2zj4.jpg|left|200px]]


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==Isomerase domain of human glucose:fructose-6-phosphate amidotransferase==
The line below this paragraph, containing "STRUCTURE_2zj4", creates the "Structure Box" on the page.
<StructureSection load='2zj4' size='340' side='right'caption='[[2zj4]], [[Resolution|resolution]] 2.20&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'>[[2zj4]] is a 1 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=2ZJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZJ4 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]] 2.2&#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=AGP:2-DEOXY-2-AMINO+GLUCITOL-6-PHOSPHATE'>AGP</scene></td></tr>
{{STRUCTURE_2zj4|  PDB=2zj4  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj4 OCA], [https://pdbe.org/2zj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zj4 RCSB], [https://www.ebi.ac.uk/pdbsum/2zj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zj4 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN] Defects in GFPT1 are the cause of myasthenia, congenital, with tubular aggregates, type 1 (CMSTA1) [MIM:[https://omim.org/entry/610542 610542]. A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.<ref>PMID:21310273</ref>
== Function ==
[https://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN] Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
== 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/zj/2zj4_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=2zj4 ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutamine:fructose-6-phosphate amidotransferase (GFAT) is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes. We now report the first structures of the isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear glucosamine-6-phosphate. The C-terminal tail including the active site displays a rigid conformation, similar to the corresponding Escherichia coli enzyme. The diversity of the CF helix near the active site suggests the helix is a major target for drug design. Our study provides insights into the development of therapeutic drugs for type 2 diabetes.


===Isomerase domain of human glucose:fructose-6-phosphate amidotransferase===
Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes.,Nakaishi Y, Bando M, Shimizu H, Watanabe K, Goto F, Tsuge H, Kondo K, Komatsu M FEBS Lett. 2009 Jan 5;583(1):163-7. Epub 2008 Dec 6. PMID:19059404<ref>PMID:19059404</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_19059404}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2zj4" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 19059404 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_19059404}}
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</StructureSection>
==About this Structure==
2ZJ4 is a 1 chain structure of sequence 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=2ZJ4 OCA].
 
==Reference==
Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes., Nakaishi Y, Bando M, Shimizu H, Watanabe K, Goto F, Tsuge H, Kondo K, Komatsu M, FEBS Lett. 2009 Jan 5;583(1):163-7. Epub 2008 Dec 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19059404 19059404]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bando, M.]]
[[Category: Large Structures]]
[[Category: Kondo, K.]]
[[Category: Bando M]]
[[Category: Nakaishi, Y.]]
[[Category: Kondo K]]
[[Category: Tsuge, H.]]
[[Category: Nakaishi Y]]
[[Category: Aldose/ketose isomerase]]
[[Category: Tsuge H]]
[[Category: Alternative splicing]]
[[Category: Aminotransferase]]
[[Category: Crystal structure]]
[[Category: Glucosamine-6-phosphate synthase]]
[[Category: Glutamine amidotransferase]]
[[Category: Phosphoprotein]]
[[Category: Rossmann-like fold]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 14 13:10:01 2009''