Metabotropic glutamate receptor

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</StructureSection>
</StructureSection>
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==3D structures of metabotropic glutamate receptor ==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*Metabotropic glutamate receptor 1
 
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**[[3ks9]] – hMGluR1 (mutant) + antagonist - human<br />
 
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**[[4or2]] - hMGluR1/cytochrome b526<br />
 
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**[[1ewt]], [[1ewv]] - rMGluR1 LBD - rat<br />
 
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**[[1isr]], [[1ewk]] – rMGluR1 LBD + Glu<br />
 
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**[[1iss]] - rMGluR1 LBD + antagonist<br />
 
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*Metabotropic glutamate receptor 2
 
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**[[4xas]], [[4xaq]] – hMGluR2 LBD + agonist<br />
 
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**[[5kzq]], [[5kzn]] – hMGluR2 LBD + antagonist<br />
 
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**[[5cni]] – hMGluR2 LBD + Glu <br />
 
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**[[5cnj]] – hMGluR2 LBD + Glu analog<br />
 
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*Metabotropic glutamate receptor 3
 
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**[[5cnk]] – hMGluR3 LBD + Glu <br />
 
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**[[3sm9]] - hMGluR3 + antagonist<br />
 
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**[[4xar]], [[6b7h]] – hMGluR3 LBD + agonist<br />
 
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**[[5cnm]] – hMGluR3 LBD + Glu analog<br />
 
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**[[2e4u]] – rMGluR3 LBD (mutant) + Glu<br />
 
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**[[2e4v]], [[2e4w]], [[2e4x]], [[2e4y]], [[2e4z]] - rMGluR3 LBD (mutant) + agonist<br />
 
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*Metabotropic glutamate receptor 5
 
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**[[6n52]] – hMGluR5 – Cryo EM<br />
 
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**[[6n51]], [[6n50]], [[6n4y]] – hMGluR5 + nanobody – Cryo EM<br />
 
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**[[6n4x]] – hMGluR5 LBD<br />
 
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**[[6ffh]], [[6ffi]] - hMGluR5 LBD (mutant) + positive allosteric modulator<br />
 
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**[[3lmk]] – hMGluR5 LBD (mutant) + positive allosteric modulator + Glu<br />
 
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**[[5cgc]], [[5cgd]] - hMGluR5 transmembrane domain + negative allosteric modulator<br />
 
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*Metabotropic glutamate receptor 7
 
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**[[5c5c]] – hMGluR7 LBD (mutant)<br />
 
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**[[3mq4]] – hMGluR7 LBD + antagonist<br />
 
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*Metabotropic glutamate receptor 8
 
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**[[6bsz]] – hMGluR8 LBD + Glu <br />
 
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**[[6bt5]] – hMGluR8 LBD + phosphonobutanoic acid <br />
 
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**[[6e5v]] – hMGluR8 N-terminal (mutant) + inhibitor <br />
 
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}}
 
==See Also==
==See Also==
[[Membrane Channels & Pumps]] <br/>
[[Membrane Channels & Pumps]] <br/>

Revision as of 09:02, 30 October 2019

Structure of the glycosylated rat binding domain of the Metabotropic Glutamate Receptor, GluR1, bound to glutamate, Hepes and Mg+2 ions (1ewk)

Drag the structure with the mouse to rotate

See Also

Membrane Channels & Pumps
Ionotropic_Glutamate_Receptors
Alzheimer's Disease

References

  1. Traynelis SF, Wollmuth LP, McBain CJ, Menniti FS, Vance KM, Ogden KK, Hansen KB, Yuan H, Myers SJ, Dingledine R. Glutamate receptor ion channels: structure, regulation, and function. Pharmacol Rev. 2010 Sep;62(3):405-96. doi: 10.1124/pr.109.002451. PMID:20716669 doi:http://dx.doi.org/10.1124/pr.109.002451
  2. Johnson KA, Conn PJ, Niswender CM. Glutamate receptors as therapeutic targets for Parkinson's disease. CNS Neurol Disord Drug Targets. 2009 Dec;8(6):475-91. PMID:19702565
  3. Niswender CM, Conn PJ. Metabotropic glutamate receptors: physiology, pharmacology, and disease. Annu Rev Pharmacol Toxicol. 2010;50:295-322. doi:, 10.1146/annurev.pharmtox.011008.145533. PMID:20055706 doi:http://dx.doi.org/10.1146/annurev.pharmtox.011008.145533
  4. Kunishima N, Shimada Y, Tsuji Y, Sato T, Yamamoto M, Kumasaka T, Nakanishi S, Jingami H, Morikawa K. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature. 2000 Oct 26;407(6807):971-7. PMID:11069170 doi:10.1038/35039564

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