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[[Image:1l1f.png|left|200px]]


{{STRUCTURE_1l1f|  PDB=1l1f  |  SCENE=  }}
==Structure of human glutamate dehydrogenase-apo form==
 
<StructureSection load='1l1f' size='340' side='right'caption='[[1l1f]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
===Structure of human glutamate dehydrogenase-apo form===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1l1f]] is a 6 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=1L1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L1F FirstGlance]. <br>
{{ABSTRACT_PUBMED_12054821}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=1l1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1f OCA], [https://pdbe.org/1l1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l1f RCSB], [https://www.ebi.ac.uk/pdbsum/1l1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l1f ProSAT]</span></td></tr>
==About this Structure==
</table>
[[1l1f]] is a 6 chain structure of [[Glutamate dehydrogenase]] with 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=1L1F OCA].  
== Disease ==
[https://www.uniprot.org/uniprot/DHE3_HUMAN DHE3_HUMAN] Defects in GLUD1 are the cause of familial hyperinsulinemic hypoglycemia type 6 (HHF6) [MIM:[https://omim.org/entry/606762 606762]; also known as hyperinsulinism-hyperammonemia syndrome (HHS). Familial hyperinsulinemic hypoglycemia [MIM:[https://omim.org/entry/256450 256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. In HHF6 elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver.<ref>PMID:9571255</ref> <ref>PMID:10636977</ref> <ref>PMID:11214910</ref> <ref>PMID:11297618</ref>
== Function ==
[https://www.uniprot.org/uniprot/DHE3_HUMAN DHE3_HUMAN] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).
== 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/l1/1l1f_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=1l1f ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Glutamate dehydrogenase|Glutamate dehydrogenase]]
*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:012054821</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Fang, J.]]
[[Category: Large Structures]]
[[Category: Schmidt, T.]]
[[Category: Fang J]]
[[Category: Siuzdak, G.]]
[[Category: Schmidt T]]
[[Category: Smith, T J.]]
[[Category: Siuzdak G]]
[[Category: Stanley, C A.]]
[[Category: Smith TJ]]
[[Category: Wu, J.]]
[[Category: Stanley CA]]
[[Category: Allostery]]
[[Category: Wu J]]
[[Category: Negative cooperativity]]
[[Category: Oxidoreductase]]

Latest revision as of 10:29, 14 February 2024

Structure of human glutamate dehydrogenase-apo formStructure of human glutamate dehydrogenase-apo form

Structural highlights

1l1f is a 6 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 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

DHE3_HUMAN Defects in GLUD1 are the cause of familial hyperinsulinemic hypoglycemia type 6 (HHF6) [MIM:606762; also known as hyperinsulinism-hyperammonemia syndrome (HHS). Familial hyperinsulinemic hypoglycemia [MIM:256450, also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. In HHF6 elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver.[1] [2] [3] [4]

Function

DHE3_HUMAN May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).

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. ↑ Stanley CA, Lieu YK, Hsu BY, Burlina AB, Greenberg CR, Hopwood NJ, Perlman K, Rich BH, Zammarchi E, Poncz M. Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med. 1998 May 7;338(19):1352-7. PMID:9571255
  2. ↑ Miki Y, Taki T, Ohura T, Kato H, Yanagisawa M, Hayashi Y. Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. J Pediatr. 2000 Jan;136(1):69-72. PMID:10636977
  3. ↑ Santer R, Kinner M, Passarge M, Superti-Furga A, Mayatepek E, Meissner T, Schneppenheim R, Schaub J. Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. Hum Genet. 2001 Jan;108(1):66-71. PMID:11214910
  4. ↑ MacMullen C, Fang J, Hsu BY, Kelly A, de Lonlay-Debeney P, Saudubray JM, Ganguly A, Smith TJ, Stanley CA. Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab. 2001 Apr;86(4):1782-7. PMID:11297618

1l1f, resolution 2.70Å

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