View source for 2lq4


==Structural Characterization of an LPA1 Second Extracellular Loop Mimetic with a Self-Assembling Coiled-Coil Folding Constraint==
<StructureSection load='2lq4' size='340' side='right'caption='[[2lq4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lq4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQ4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq4 OCA], [https://pdbe.org/2lq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lq4 RCSB], [https://www.ebi.ac.uk/pdbsum/2lq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lq4 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
G protein-coupled receptor (GPCR) structures are of interest as a means to understand biological signal transduction and as tools for therapeutic discovery. The growing number of GPCR crystal structures demonstrates that the extracellular loops (EL) connecting the membrane-spanning helices show tremendous structural variability relative to the more structurally-conserved seven transmembrane alpha-helical domains. The EL of the LPA(1) receptor have not yet been conclusively resolved, and bear limited sequence identity to known structures. This study involved development of a peptide to characterize the intrinsic structure of the LPA(1) GPCR second EL. The loop was embedded between two helices that assemble into a coiled-coil, which served as a receptor-mimetic folding constraint (LPA(1)-CC-EL2 peptide). The ensemble of structures from multi-dimensional NMR experiments demonstrated that a robust coiled-coil formed without noticeable deformation due to the EL2 sequence. In contrast, the EL2 sequence showed well-defined structure only near its C-terminal residues. The NMR ensemble was combined with a computational model of the LPA(1) receptor that had previously been validated. The resulting hybrid models were evaluated using docking. Nine different hybrid models interacted with LPA 18:1 as expected, based on prior mutagenesis studies, and one was additionally consistent with antagonist affinity trends.

Structural Characterization of an LPA1 Second Extracellular Loop Mimetic with a Self-Assembling Coiled-Coil Folding Constraint.,Young JK, Clayton BT, Kikonyogo A, Pham TC, Parrill AL Int J Mol Sci. 2013 Jan 29;14(2):2788-807. doi: 10.3390/ijms14022788. PMID:23434648<ref>PMID:23434648</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2lq4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lysophosphatidic acid receptor|Lysophosphatidic acid receptor]]
*[[Sandbox Reserved 1789|Sandbox Reserved 1789]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Young JK]]