5glh

From Proteopedia

(Difference between revisions)

Revision as of 11:35, 2 August 2023

Human endothelin receptor type-B in complex with ET-1

Structural highlights

5glh is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
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, a 21-amino-acid peptide, participates in various physiological processes, such as regulation of vascular tone, humoral homeostasis, neural crest cell development and neurotransmission. Endothelin and its G-protein-coupled receptor are involved in the development of various diseases, such as pulmonary arterial hypertension, and thus are important therapeutic targets. Here we report crystal structures of human endothelin type B receptor in the ligand-free form and in complex with the endogenous agonist endothelin-1. The structures and mutation analysis reveal the mechanism for the isopeptide selectivity between endothelin-1 and -3. Transmembrane helices 1, 2, 6 and 7 move and envelop the entire endothelin peptide, in a virtually irreversible manner. The agonist-induced conformational changes are propagated to the receptor core and the cytoplasmic G-protein coupling interface, and probably induce conformational flexibility in TM6. A comparison with the M2 muscarinic receptor suggests a shared mechanism for signal transduction in class A G-protein-coupled receptors.

Activation mechanism of endothelin ETB receptor by endothelin-1.,Shihoya W, Nishizawa T, Okuta A, Tani K, Dohmae N, Fujiyoshi Y, Nureki O, Doi T Nature. 2016 Sep 5;537(7620):363-368. doi: 10.1038/nature19319. PMID:27595334^[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
↑ Shihoya W, Nishizawa T, Okuta A, Tani K, Dohmae N, Fujiyoshi Y, Nureki O, Doi T. Activation mechanism of endothelin ETB receptor by endothelin-1. Nature. 2016 Sep 5;537(7620):363-368. doi: 10.1038/nature19319. PMID:27595334 doi:http://dx.doi.org/10.1038/nature19319

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/5glh"

@@ Line 3: / Line 3: @@
 <StructureSection load='5glh' size='340' side='right'caption='[[5glh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5glh]] 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=5GLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GLH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5glh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GLH FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gli|5gli]]</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]] 2.8&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EDNRB ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5glh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5glh OCA], [https://pdbe.org/5glh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5glh RCSB], [https://www.ebi.ac.uk/pdbsum/5glh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5glh 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=5glh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5glh OCA], [http://pdbe.org/5glh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5glh RCSB], [http://www.ebi.ac.uk/pdbsum/5glh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5glh ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[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/EDN1_HUMAN EDN1_HUMAN]] Endothelins are endothelium-derived vasoconstrictor peptides.
+[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 23: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Dohmae, N]]
+[[Category: Dohmae N]]
-[[Category: Doi, T]]
+[[Category: Doi T]]
-[[Category: Fujiyoshi, Y]]
+[[Category: Fujiyoshi Y]]
-[[Category: Nishizawa, T]]
+[[Category: Nishizawa T]]
-[[Category: Nureki, O]]
+[[Category: Nureki O]]
-[[Category: Okuta, A]]
+[[Category: Okuta A]]
-[[Category: Shihoya, W]]
+[[Category: Shihoya W]]
-[[Category: Tani, K]]
+[[Category: Tani K]]
-[[Category: Alpha helical]]
-[[Category: Signaling protein]]

5glh

From Proteopedia

Revision as of 11:35, 2 August 2023

Human endothelin receptor type-B in complex with ET-1

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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