Metabotropic glutamate receptor: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 1: Line 1:
<Structure load='1ewk' size='350' side='right' caption='Structure of the binding domain of the Metabotropic Glutamate Receptor, GluR1, bound to glutamate and gadolinium ions ([[1isr]])' scene=' '/>
<Structure load='1ewk' size='350' side='right' caption='Structure of the glycosylated rat binding domain of the Metabotropic Glutamate Receptor, GluR1, bound to glutamate, Hepes and Mg+2 ions ([[1ewk]])' scene=' '/>
== Function ==
[[Metabotropic glutamate receptor|Metabotropic glutamate receptors]] are [[Glutamate Receptors|glutamate receptors]] that activate ion channels indirectly through a signaling cascade involving G proteins<ref>PMID:20716669</ref>. They are members of the large class of seven-transmembrane domain receptors, the [[G protein-coupled receptor|G protein-coupled receptors]]. Glutamate receptors are classified into 3 groups based on their homology, mechanism and pharmacological properties.  See also [[Ligand Binding N-Terminal of Metabotropic Glutamate Receptors]].
[[Metabotropic glutamate receptor|Metabotropic glutamate receptors]] are [[Glutamate Receptors|glutamate receptors]] that activate ion channels indirectly through a signaling cascade involving G proteins<ref>PMID:20716669</ref>. They are members of the large class of seven-transmembrane domain receptors, the [[G protein-coupled receptor|G protein-coupled receptors]]. Glutamate receptors are classified into 3 groups based on their homology, mechanism and pharmacological properties.  See also [[Ligand Binding N-Terminal of Metabotropic Glutamate Receptors]].


Line 10: Line 11:
*[[Membrane proteins]]
*[[Membrane proteins]]
<br />
<br />
== Structural highlights ==
Glutamate is bound to GluR1 in the crevice between the N-terminal and C-terminal domains<ref>PMID:11069170</ref>.
==3D structures of metabotropic glutamate receptor ==
==3D structures of metabotropic glutamate receptor ==



Revision as of 12:17, 21 April 2016

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

FunctionFunction

Metabotropic glutamate receptors are glutamate receptors that activate ion channels indirectly through a signaling cascade involving G proteins[1]. They are members of the large class of seven-transmembrane domain receptors, the G protein-coupled receptors. Glutamate receptors are classified into 3 groups based on their homology, mechanism and pharmacological properties. See also Ligand Binding N-Terminal of Metabotropic Glutamate Receptors.

  • Metabotropic glutamate receptor 1 and metabotropic glutamate receptor 5 belong to group I and activate phospholipase C.
  • Metabotropic glutamate receptor 2 and metabotropic glutamate receptor 3 belong to group II and inhibit the cyclic AMP cascade.
  • Metabotropic glutamate receptor 7 belongs to group III and inhibits adenylate cyclase activity.

Articles in Proteopedia concerning Toll-like Receptors include:


Structural highlightsStructural highlights

Glutamate is bound to GluR1 in the crevice between the N-terminal and C-terminal domains[2].

3D structures of metabotropic glutamate receptor3D structures of metabotropic glutamate receptor

Updated on 21-April-2016

See AlsoSee Also

Membrane Channels & Pumps
Ionotropic_Glutamate_Receptors
Alzheimer's Disease

ReferencesReferences

  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. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Michal Harel, Nikki Hunter, Alexander Berchansky