3pmx

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Current revision (02:16, 21 November 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pmx OCA], [https://pdbe.org/3pmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pmx RCSB], [https://www.ebi.ac.uk/pdbsum/3pmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pmx ProSAT]</span></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=3pmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pmx OCA], [https://pdbe.org/3pmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pmx RCSB], [https://www.ebi.ac.uk/pdbsum/3pmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pmx ProSAT]</span></td></tr>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/GRIA2_RAT GRIA2_RAT] Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.<ref>PMID:9351977</ref> <ref>PMID:19265014</ref> <ref>PMID:21172611</ref> <ref>PMID:12501192</ref> <ref>PMID:12015593</ref> <ref>PMID:12872125</ref> <ref>PMID:12730367</ref> <ref>PMID:16192394</ref> <ref>PMID:15591246</ref> <ref>PMID:17018279</ref> <ref>PMID:16483599</ref> <ref>PMID:19946266</ref> <ref>PMID:21317873</ref> <ref>PMID:21846932</ref>
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== Publication Abstract from PubMed ==
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Starting from compound 1, we utilized biostructural data to successfully evolve an existing series into a new chemotype with a promising overall profile, exemplified by 19.
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Structure based evolution of a novel series of positive modulators of the AMPA receptor.,Jamieson C, Maclean JK, Brown CI, Campbell RA, Gillen KJ, Gillespie J, Kazemier B, Kiczun M, Lamont Y, Lyons AJ, Moir EM, Morrow JA, Pantling J, Rankovic Z, Smith L Bioorg Med Chem Lett. 2011 Jan 15;21(2):805-11. Epub 2010 Nov 25. PMID:21190850<ref>PMID:21190850</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3pmx" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==

Current revision

Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator

PDB ID 3pmx

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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