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8aqt

From Proteopedia

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Current revision

Beta SARS-CoV-2 Spike bound to mouse ACE2 (local)

Structural highlights

8aqt is a 2 chain structure with sequence from Escherichia virus T4, Mus musculus and Severe acute respiratory syndrome coronavirus 2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACE2_MOUSE Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A (By similarity). By cleavage of angiotensin II, may be an important regulator of heart function (PubMed:12075344, PubMed:12967627). By cleavage of angiotensin II, may also have a protective role in acute lung injury (PubMed:16001071). Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19, regulating its trafficking on the cell surface and its activity (PubMed:19185582, PubMed:18424768, PubMed:22677001).[UniProtKB:Q9BYF1]^[1] ^[2] ^[3] ^[4] ^[5] ^[6] GCAM_MOUSE

References

↑ Crackower MA, Sarao R, Oudit GY, Yagil C, Kozieradzki I, Scanga SE, Oliveira-dos-Santos AJ, da Costa J, Zhang L, Pei Y, Scholey J, Ferrario CM, Manoukian AS, Chappell MC, Backx PH, Yagil Y, Penninger JM. Angiotensin-converting enzyme 2 is an essential regulator of heart function. Nature. 2002 Jun 20;417(6891):822-8. PMID:12075344 doi:http://dx.doi.org/10.1038/nature00786
↑ Donoghue M, Wakimoto H, Maguire CT, Acton S, Hales P, Stagliano N, Fairchild-Huntress V, Xu J, Lorenz JN, Kadambi V, Berul CI, Breitbart RE. Heart block, ventricular tachycardia, and sudden death in ACE2 transgenic mice with downregulated connexins. J Mol Cell Cardiol. 2003 Sep;35(9):1043-53. PMID:12967627
↑ Imai Y, Kuba K, Rao S, Huan Y, Guo F, Guan B, Yang P, Sarao R, Wada T, Leong-Poi H, Crackower MA, Fukamizu A, Hui CC, Hein L, Uhlig S, Slutsky AS, Jiang C, Penninger JM. Angiotensin-converting enzyme 2 protects from severe acute lung failure. Nature. 2005 Jul 7;436(7047):112-6. PMID:16001071 doi:http://dx.doi.org/nature03712
↑ Kowalczuk S, Broer A, Tietze N, Vanslambrouck JM, Rasko JE, Broer S. A protein complex in the brush-border membrane explains a Hartnup disorder allele. FASEB J. 2008 Aug;22(8):2880-7. doi: 10.1096/fj.08-107300. Epub 2008 Apr 18. PMID:18424768 doi:http://dx.doi.org/10.1096/fj.08-107300
↑ Camargo SM, Singer D, Makrides V, Huggel K, Pos KM, Wagner CA, Kuba K, Danilczyk U, Skovby F, Kleta R, Penninger JM, Verrey F. Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. Gastroenterology. 2009 Mar;136(3):872-82. doi: 10.1053/j.gastro.2008.10.055. Epub, 2008 Oct 29. PMID:19185582 doi:http://dx.doi.org/10.1053/j.gastro.2008.10.055
↑ Fairweather SJ, Broer A, O'Mara ML, Broer S. Intestinal peptidases form functional complexes with the neutral amino acid transporter B(0)AT1. Biochem J. 2012 Aug 15;446(1):135-48. doi: 10.1042/BJ20120307. PMID:22677001 doi:http://dx.doi.org/10.1042/BJ20120307

1 Structural highlights
2 Function
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8aqt"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8aqt is ON HOLD
+==Beta SARS-CoV-2 Spike bound to mouse ACE2 (local)==
+<StructureSection load='8aqt' size='340' side='right'caption='[[8aqt]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8aqt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AQT FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8aqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aqt OCA], [https://pdbe.org/8aqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aqt RCSB], [https://www.ebi.ac.uk/pdbsum/8aqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aqt ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACE2_MOUSE ACE2_MOUSE] Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A (By similarity). By cleavage of angiotensin II, may be an important regulator of heart function (PubMed:12075344, PubMed:12967627). By cleavage of angiotensin II, may also have a protective role in acute lung injury (PubMed:16001071). Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19, regulating its trafficking on the cell surface and its activity (PubMed:19185582, PubMed:18424768, PubMed:22677001).[UniProtKB:Q9BYF1]<ref>PMID:12075344</ref> <ref>PMID:12967627</ref> <ref>PMID:16001071</ref> <ref>PMID:18424768</ref> <ref>PMID:19185582</ref> <ref>PMID:22677001</ref> [https://www.uniprot.org/uniprot/GCAM_MOUSE GCAM_MOUSE]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia virus T4]]
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Severe acute respiratory syndrome coronavirus 2]]
+[[Category: Alexander M]]
+[[Category: Bertrand B]]
+[[Category: Dong CN]]
+[[Category: Emiko U]]
+[[Category: Florence P]]
+[[Category: Henning S]]
+[[Category: Kelvin L]]
+[[Category: Sergey N]]

8aqt

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Current revision

Beta SARS-CoV-2 Spike bound to mouse ACE2 (local)

Structural highlights

Function

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