User:Wayne Decatur/Sandbox Glutamate receptor: Difference between revisions
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The [http://en.wikipedia.org/wiki/Glutamate_receptor glutamate receptor]is the ion channel opened by glutamate that keeps neurons in touch by mediating fast cell-to-cell information transfer in the nervous system. Several studies have revealed structures for portions of the glutamate receptor <ref name="r80">PMID: 19461580</ref><ref name="r14">PMID: 19465914</ref><ref name="r22">PMID: 19910922</ref><ref>PMID: 9804426</ref>. Groundbreaking work elucidated the structure of a complete functional, homomeric glutamate receptor<ref name="main">PMID:19946266</ref><ref>PMID: 20010675</ref> and that structure, [[3kg2]], is the subject of this page. | The [http://en.wikipedia.org/wiki/Glutamate_receptor glutamate receptor]is the ion channel opened by glutamate that keeps neurons in touch by mediating fast cell-to-cell information transfer in the nervous system. Several studies have revealed structures for portions of the glutamate receptor <ref name="r80">PMID: 19461580</ref><ref name="r14">PMID: 19465914</ref><ref name="r22">PMID: 19910922</ref><ref>PMID: 9804426</ref>. Groundbreaking work elucidated the structure of a complete functional, homomeric glutamate receptor<ref name="main">PMID:19946266</ref><ref>PMID: 20010675</ref> and that structure, [[3kg2]], is the subject of this page. | ||
==Structure of the Glutamate Receptor (GluA2)== | ==Structure of the Glutamate Receptor (GluA2)== | ||
{{Structure | {{Structure | ||
|PDB= 3kg2 |SIZE=400|SCENE=User:Wayne_Decatur/Sandbox_Glutamate_receptor/Default3kg2/1|CAPTION= glutamate receptor ([[3kg2]]), resolution 3.6Å (<scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Default3kg2/1'>initial scene</scene>) | |PDB= 3kg2 |SIZE=400|SCENE=User:Wayne_Decatur/Sandbox_Glutamate_receptor/Default3kg2/1|CAPTION= glutamate receptor ([[3kg2]]), resolution 3.6Å (<scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Default3kg2/1'>initial scene</scene>) | ||
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|RELATEDENTRY= | |RELATEDENTRY= | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg2 OCA], [http://www.ebi.ac.uk/pdbsum/3kg2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3kg2 RCSB]</span> | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg2 OCA], [http://www.ebi.ac.uk/pdbsum/3kg2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3kg2 RCSB]</span> | ||
}} | }}The homomeric rat GluA2 receptor <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Default3kg2/1'>has four subunits</scene> arranged in a 'Y'-shape with the <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Meas3kg2/1'>'top' being about three times the width of the 'bottom'</scene><ref name="main" />. This structure is a functional homotetramer of the AMPA-subtype; native ionotropic glutamate receptors are almost exclusively heterotetramers. {{Link Toggle FancyCartoonHighQualityView}}. | ||
===Domains=== | ===Domains=== | ||
The subunits themselves are modular <ref>PMID: 7539962</ref>and the major domains are found in layers in the tetrameric structure. | The subunits themselves are modular <ref>PMID: 7539962</ref>and the major domains are found in layers in the tetrameric structure. | ||
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<scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Atobmorph/2'>Subunit A morphing into Subunit B best illustrates how portions, especially the linkers, of the protein change</scene> between the two conformational forms.<br> | <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Atobmorph/2'>Subunit A morphing into Subunit B best illustrates how portions, especially the linkers, of the protein change</scene> between the two conformational forms.<br> | ||
{{Button Toggle AnimationOnPause}} | {{Button Toggle AnimationOnPause}} | ||
:The linkers are key; besides playing roles in domain swapping and resolving the symmetry mismatch, they are also responsible for relaying the modulation signals from the ATD to the other domains and signaling the conformational change of the LBD to control the opening and closing of the pore. Beyond the two conformations seen here though this particular structure ([[3kg2]]) of the receptor does not shed light on the transduction process. | |||
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* [http://www.nature.com/nature/journal/v462/n7274/covers/ Glutamate Receptor on the cover] of [http://www.nature.com/ Nature] | * [http://www.nature.com/nature/journal/v462/n7274/covers/ Glutamate Receptor on the cover] of [http://www.nature.com/ Nature] | ||
* [http://en.wikipedia.org/wiki/Glutamate_receptor Glutamate receptor Wikipedia entry] | * [http://en.wikipedia.org/wiki/Glutamate_receptor Glutamate receptor Wikipedia entry] | ||
* [http://www.bristol.ac.uk/synaptic/receptors/#ionotropic Glutamate Receptors page] at the [http://www.bristol.ac.uk/synaptic/ MRC Centre for Synaptic Plasticity at the University of Bristol] | |||
''Page started with original page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 16 11:24:54 2009 for [[3kg2]].'' | ''Page started with original page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 16 11:24:54 2009 for [[3kg2]].'' | ||
