8hnm
From Proteopedia
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<table><tr><td colspan='2'>[[8hnm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oplophorus_gracilirostris Oplophorus gracilirostris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HNM FirstGlance]. <br> | <table><tr><td colspan='2'>[[8hnm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oplophorus_gracilirostris Oplophorus gracilirostris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HNM FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.94Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.94Å</td></tr> | ||
| - | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4IE:[4-(2-bromophenyl)phenyl]methyl-[[( | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4IE:[4-(2-bromophenyl)phenyl]methyl-[[(1~{R},5~{S})-6,6-dimethyl-2-bicyclo[3.1.1]hept-2-enyl]methyl]-dimethyl-azanium'>4IE</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</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=8hnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hnm OCA], [https://pdbe.org/8hnm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hnm RCSB], [https://www.ebi.ac.uk/pdbsum/8hnm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hnm 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=8hnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hnm OCA], [https://pdbe.org/8hnm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hnm RCSB], [https://www.ebi.ac.uk/pdbsum/8hnm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hnm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GNAI1_HUMAN GNAI1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:17635935</ref> <ref>PMID:17264214</ref> | [https://www.uniprot.org/uniprot/GNAI1_HUMAN GNAI1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:17635935</ref> <ref>PMID:17264214</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The chemotaxis of CD4(+) type 1 helper cells and CD8(+) cytotoxic lymphocytes, guided by interferon-inducible CXC chemokine 9-11 (CXCL9-11) and CXC chemokine receptor 3 (CXCR3), plays a critical role in type 1 immunity. Here we determined the structures of human CXCR3-DNG(i) complexes activated by chemokine CXCL11, peptidomimetic agonist PS372424 and biaryl-type agonist VUF11222, and the structure of inactive CXCR3 bound to noncompetitive antagonist SCH546738. Structural analysis revealed that PS372424 shares a similar orthosteric binding pocket to the N terminus of CXCL11, while VUF11222 buries deeper and activates the receptor in a distinct manner. We showed an allosteric binding site between TM5 and TM6, accommodating SCH546738 in the inactive CXCR3. SCH546738 may restrain the receptor at an inactive state by preventing the repacking of TM5 and TM6. By revealing the binding patterns and the pharmacological properties of the four modulators, we present the activation mechanisms of CXCR3 and provide insights for future drug development. | ||
| + | |||
| + | Structural insights into the activation and inhibition of CXC chemokine receptor 3.,Jiao H, Pang B, Liu A, Chen Q, Pan Q, Wang X, Xu Y, Chiang YC, Ren R, Hu H Nat Struct Mol Biol. 2024 Apr;31(4):610-620. doi: 10.1038/s41594-023-01175-5. , Epub 2024 Jan 4. PMID:38177682<ref>PMID:38177682</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8hnm" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
CXCR3-DNGi complex activated by VUF11222
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