3zpr: Difference between revisions
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==Thermostabilised turkey beta1 adrenergic receptor with 4-methyl-2-(piperazin-1-yl) quinoline bound== | |||
<StructureSection load='3zpr' size='340' side='right'caption='[[3zpr]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZPR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=3WC:4-METHYL-2-(PIPERAZIN-1-YL)+QUINOLINE'>3WC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></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=3zpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zpr OCA], [https://pdbe.org/3zpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zpr RCSB], [https://www.ebi.ac.uk/pdbsum/3zpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zpr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ADRB1_MELGA ADRB1_MELGA] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Biophysical fragment screening of a thermostabilised beta1-adrenergic receptor (beta1AR) using surface plasmon resonance (SPR) enabled the identification of moderate affinity, high ligand efficiency (LE) phenyl piperazine hits 7 and 8. Subsequent hit to lead follow up confirmed the activity of the chemotype and a structure-based design approach using protein-ligand crystal structures of the beta1AR resulted in the identification of several fragments that bound with higher affinity, including indole 19 and quinoline 20. In the first example of GPCR crystallography with ligands derived from fragment screening, structures of the stabilised beta1AR complexed with 19 and 20 were determined at resolutions of 2.8A and 2.7A, respectively. | |||
Biophysical fragment screening of the beta1-adrenergic receptor: Identification of high affinity aryl piperazine leads using structure-based drug design.,Christopher J, Brown J, Dore A, Errey J, Koglin M, Marshall FH, Myszka D, Rich RL, Tate CG, Tehan B, Warne T, Congreve M J Med Chem. 2013 Mar 21. PMID:23517028<ref>PMID:23517028</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zpr" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Meleagris gallopavo]] | |||
[[Category: Brown J]] | |||
[[Category: Christopher JA]] | |||
[[Category: Congreve M]] | |||
[[Category: Dore AS]] | |||
[[Category: Errey JC]] | |||
[[Category: Koglin M]] | |||
[[Category: Marshall FH]] | |||
[[Category: Myszka DG]] | |||
[[Category: Tate CG]] | |||
[[Category: Tehan B]] | |||
[[Category: Warne T]] | |||
Latest revision as of 14:09, 20 December 2023
Thermostabilised turkey beta1 adrenergic receptor with 4-methyl-2-(piperazin-1-yl) quinoline boundThermostabilised turkey beta1 adrenergic receptor with 4-methyl-2-(piperazin-1-yl) quinoline bound
Structural highlights
FunctionADRB1_MELGA Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Publication Abstract from PubMedBiophysical fragment screening of a thermostabilised beta1-adrenergic receptor (beta1AR) using surface plasmon resonance (SPR) enabled the identification of moderate affinity, high ligand efficiency (LE) phenyl piperazine hits 7 and 8. Subsequent hit to lead follow up confirmed the activity of the chemotype and a structure-based design approach using protein-ligand crystal structures of the beta1AR resulted in the identification of several fragments that bound with higher affinity, including indole 19 and quinoline 20. In the first example of GPCR crystallography with ligands derived from fragment screening, structures of the stabilised beta1AR complexed with 19 and 20 were determined at resolutions of 2.8A and 2.7A, respectively. Biophysical fragment screening of the beta1-adrenergic receptor: Identification of high affinity aryl piperazine leads using structure-based drug design.,Christopher J, Brown J, Dore A, Errey J, Koglin M, Marshall FH, Myszka D, Rich RL, Tate CG, Tehan B, Warne T, Congreve M J Med Chem. 2013 Mar 21. PMID:23517028[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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