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6k1q

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Current revision

Human endothelin receptor type-B in complex with inverse agonist IRL2500

Structural highlights

6k1q is a 1 chain structure with sequence from Escherichia virus T4 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

EDNRB_HUMAN Hirschsprung disease;Waardenburg-Shah syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Defects in EDNRB are associated with Waardenburg syndrome 2, with ocular albinism, autosomal recessive: A disorder characterized by the association of features typical of Waardenburg syndrome type 2 with ocular albinism. Patients manifest reduced visual acuity, albinotic fundus, deafness, hypomelanosis.^[1]

Function

ENLYS_BPT4 Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.^[2] EDNRB_HUMAN Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.^[3]

Publication Abstract from PubMed

Endothelin receptors (ETA and ETB) are G-protein-coupled receptors activated by endothelin-1 and are involved in blood pressure regulation. IRL2500 is a peptide-mimetic of the C-terminal tripeptide of endothelin-1, and has been characterized as a potent ETB-selective antagonist, which has preventive effects against brain edema. Here, we report the crystal structure of the human ETB receptor in complex with IRL2500 at 2.7 A-resolution. The structure revealed the different binding modes between IRL2500 and endothelin-1, and provides structural insights into its ETB-selectivity. Notably, the biphenyl group of IRL2500 penetrates into the transmembrane core proximal to D(2.50), thus stabilizing the inactive conformation. Using the newly-established constitutively active mutant, we clearly demonstrate that IRL2500 functions as an inverse agonist for the ETB receptor. The current findings will expand the chemical space of ETR antagonists and facilitate the design of inverse agonists for other class A GPCRs.

Crystal structure of human endothelin ETB receptor in complex with peptide inverse agonist IRL2500.,Nagiri C, Shihoya W, Inoue A, Kadji FMN, Aoki J, Nureki O Commun Biol. 2019 Jun 21;2:236. doi: 10.1038/s42003-019-0482-7. eCollection 2019. PMID:31263780^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Issa S, Bondurand N, Faubert E, Poisson S, Lecerf L, Nitschke P, Deggouj N, Loundon N, Jonard L, David A, Sznajer Y, Blanchet P, Marlin S, Pingault V. EDNRB mutations cause Waardenburg syndrome type II in the heterozygous state. Hum Mutat. 2017 May;38(5):581-593. doi: 10.1002/humu.23206. Epub 2017 Mar 15. PMID:28236341 doi:http://dx.doi.org/10.1002/humu.23206
↑ Moussa SH, Kuznetsov V, Tran TA, Sacchettini JC, Young R. Protein determinants of phage T4 lysis inhibition. Protein Sci. 2012 Apr;21(4):571-82. doi: 10.1002/pro.2042. Epub 2012 Mar 2. PMID:22389108 doi:http://dx.doi.org/10.1002/pro.2042
↑ Webb ML, Chao CC, Rizzo M, Shapiro RA, Neubauer M, Liu EC, Aversa CR, Brittain RJ, Treiger B. Cloning and expression of an endothelin receptor subtype B from human prostate that mediates contraction. Mol Pharmacol. 1995 Apr;47(4):730-7. PMID:7536888
↑ Nagiri C, Shihoya W, Inoue A, Kadji FMN, Aoki J, Nureki O. Crystal structure of human endothelin ETB receptor in complex with peptide inverse agonist IRL2500. Commun Biol. 2019 Jun 21;2:236. doi: 10.1038/s42003-019-0482-7. eCollection 2019. PMID:31263780 doi:http://dx.doi.org/10.1038/s42003-019-0482-7

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6k1q"

@@ Line 3: / Line 3: @@
 <StructureSection load='6k1q' size='340' side='right'caption='[[6k1q]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6k1q]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K1Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6k1q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K1Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D2U:(2~{S})-2-[[(2~{R})-2-[(3,5-dimethylphenyl)carbonyl-methyl-amino]-3-(4-phenylphenyl)propanoyl]amino]-3-(1~{H}-indol-3-yl)propanoic+acid'>D2U</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D2U:(2~{S})-2-[[(2~{R})-2-[(3,5-dimethylphenyl)carbonyl-methyl-amino]-3-(4-phenylphenyl)propanoyl]amino]-3-(1~{H}-indol-3-yl)propanoic+acid'>D2U</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=6k1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k1q OCA], [http://pdbe.org/6k1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k1q RCSB], [http://www.ebi.ac.uk/pdbsum/6k1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k1q 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=6k1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k1q OCA], [https://pdbe.org/6k1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k1q RCSB], [https://www.ebi.ac.uk/pdbsum/6k1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k1q ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/EDNRB_HUMAN EDNRB_HUMAN]] Hirschsprung disease;Waardenburg-Shah syndrome. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  Defects in EDNRB are associated with Waardenburg syndrome 2, with ocular albinism, autosomal recessive: A disorder characterized by the association of features typical of Waardenburg syndrome type 2 with ocular albinism. Patients manifest reduced visual acuity, albinotic fundus, deafness, hypomelanosis.<ref>PMID:28236341</ref>
+[https://www.uniprot.org/uniprot/EDNRB_HUMAN EDNRB_HUMAN] Hirschsprung disease;Waardenburg-Shah syndrome. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  Defects in EDNRB are associated with Waardenburg syndrome 2, with ocular albinism, autosomal recessive: A disorder characterized by the association of features typical of Waardenburg syndrome type 2 with ocular albinism. Patients manifest reduced visual acuity, albinotic fundus, deafness, hypomelanosis.<ref>PMID:28236341</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/EDNRB_HUMAN EDNRB_HUMAN]] Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.<ref>PMID:7536888</ref>
+[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> [https://www.uniprot.org/uniprot/EDNRB_HUMAN EDNRB_HUMAN] Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.<ref>PMID:7536888</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Escherichia virus T4]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Lysozyme]]
+[[Category: Nagiri C]]
-[[Category: Nagiri, C]]
+[[Category: Nureki O]]
-[[Category: Nureki, O]]
+[[Category: Shihoya W]]
-[[Category: Shihoya, W]]
-[[Category: Alpha helical]]
-[[Category: Signaling protein]]

6k1q

From Proteopedia

Current revision

Human endothelin receptor type-B in complex with inverse agonist IRL2500

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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