2e4z: Difference between revisions
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|PDB= 2e4z |SIZE=350|CAPTION= <scene name='initialview01'>2e4z</scene>, resolution 3.30Å | |PDB= 2e4z |SIZE=350|CAPTION= <scene name='initialview01'>2e4z</scene>, resolution 3.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2e4u|2E4U]], [[2e4v|2E4V]], [[2e4w|2E4W]], [[2e4x|2E4X]], [[2e4y|2E4Y]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4z OCA], [http://www.ebi.ac.uk/pdbsum/2e4z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e4z RCSB]</span> | |||
}} | }} | ||
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[[Category: Muto, T.]] | [[Category: Muto, T.]] | ||
[[Category: Tsuchiya, D.]] | [[Category: Tsuchiya, D.]] | ||
[[Category: central nerve system]] | [[Category: central nerve system]] | ||
[[Category: g-protein-coupled receptor]] | [[Category: g-protein-coupled receptor]] | ||
[[Category: neuron]] | [[Category: neuron]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:43:51 2008'' | ||
Revision as of 02:43, 31 March 2008
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| , resolution 3.30Å | |||||||
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| Ligands: | |||||||
| Related: | 2E4U, 2E4V, 2E4W, 2E4X, 2E4Y
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the ligand-binding region of the group III metabotropic glutamate receptor
OverviewOverview
Metabotropic glutamate receptors play major roles in the activation of excitatory synapses in the central nerve system. We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor. A comparison among groups I, II, and III provides the structural basis that could account for the discrimination of group-specific agonists. Furthermore, the structure of group II includes the cysteine-rich domain, which is tightly linked to the ligand-binding domain by a disulfide bridge, suggesting a potential role in transmitting a ligand-induced conformational change into the downstream transmembrane region. The structure also reveals the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of the dimeric receptors on the cell surface. We propose a general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements.
About this StructureAbout this Structure
2E4Z is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors., Muto T, Tsuchiya D, Morikawa K, Jingami H, Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:17360426
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