6bt5: Difference between revisions
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<StructureSection load='6bt5' size='340' side='right' caption='[[6bt5]], [[Resolution|resolution]] 2.92Å' scene=''> | <StructureSection load='6bt5' size='340' side='right' caption='[[6bt5]], [[Resolution|resolution]] 2.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6bt5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BT5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6bt5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BT5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E7P:(2S)-2-amino-4-phosphonobutanoic+acid'>E7P</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E7P:(2S)-2-amino-4-phosphonobutanoic+acid'>E7P</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRM8, GPRC1H, MGLUR8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bt5 OCA], [http://pdbe.org/6bt5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bt5 RCSB], [http://www.ebi.ac.uk/pdbsum/6bt5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bt5 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bt5 OCA], [http://pdbe.org/6bt5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bt5 RCSB], [http://www.ebi.ac.uk/pdbsum/6bt5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bt5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/GRM8_HUMAN GRM8_HUMAN]] G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.<ref>PMID:9473604</ref> | [[http://www.uniprot.org/uniprot/GRM8_HUMAN GRM8_HUMAN]] G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.<ref>PMID:9473604</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
L-2-Amino-4-phosphonobutyric acid (L-AP4) is a known potent and selective agonist for the Group III mGlu receptors. However, it does not show any selectivity among the individual group III mGlu subtypes. In order to understand the molecular basis for this group selectivity, we solved the first human mGlu8 amino terminal domain (ATD) crystal structures in complex with L-glu and L-AP4. In comparison with other published L-glu-bound mGlu ATD structures, we have observed L-glu binds in a significantly different manner in mGlu1. Furthermore, these new structures provided evidence that both the electronic and steric nature of the distal phosphate of L-AP4 contribute to its exquisite Group III functional agonist potency and selectivity. | |||
Determination of L-AP4-bound human mGlu8 receptor amino terminal domain structure and the molecular basis for L-AP4's group III mGlu receptor functional potency and selectivity.,Schkeryantz JM, Chen Q, Ho JD, Atwell S, Zhang A, Vargas MC, Wang J, Monn JA, Hao J Bioorg Med Chem Lett. 2018 Feb 15;28(4):612-617. doi: 10.1016/j.bmcl.2018.01.037., Epub 2018 Jan 31. PMID:29402739<ref>PMID:29402739</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6bt5" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Atwell, S]] | [[Category: Atwell, S]] | ||
[[Category: Chen, Q]] | [[Category: Chen, Q]] | ||
Revision as of 11:28, 22 February 2018
Human mGlu8 Receptor complexed with L-AP4Human mGlu8 Receptor complexed with L-AP4
Structural highlights
Function[GRM8_HUMAN] G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.[1] Publication Abstract from PubMedL-2-Amino-4-phosphonobutyric acid (L-AP4) is a known potent and selective agonist for the Group III mGlu receptors. However, it does not show any selectivity among the individual group III mGlu subtypes. In order to understand the molecular basis for this group selectivity, we solved the first human mGlu8 amino terminal domain (ATD) crystal structures in complex with L-glu and L-AP4. In comparison with other published L-glu-bound mGlu ATD structures, we have observed L-glu binds in a significantly different manner in mGlu1. Furthermore, these new structures provided evidence that both the electronic and steric nature of the distal phosphate of L-AP4 contribute to its exquisite Group III functional agonist potency and selectivity. Determination of L-AP4-bound human mGlu8 receptor amino terminal domain structure and the molecular basis for L-AP4's group III mGlu receptor functional potency and selectivity.,Schkeryantz JM, Chen Q, Ho JD, Atwell S, Zhang A, Vargas MC, Wang J, Monn JA, Hao J Bioorg Med Chem Lett. 2018 Feb 15;28(4):612-617. doi: 10.1016/j.bmcl.2018.01.037., Epub 2018 Jan 31. PMID:29402739[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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