8bfw: Difference between revisions

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'''Unreleased structure'''


The entry 8bfw is ON HOLD
==The structures of Ace2 in complex with bicyclic peptide inhibitor==
 
<StructureSection load='8bfw' size='340' side='right'caption='[[8bfw]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
Authors: Brear, P., Lulla, A., Harman, M., Dods, R., Chen, L., Bezerra, G., Demydchuk, Y., Stanway, S., Hyvonen, M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8bfw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BFW FirstGlance]. <br>
Description: The structures of Ace2 in complex with bicyclic peptide inhibitor
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LFI:1-[3,5-bis(3-bromanylpropanoyl)-1,3,5-triazinan-1-yl]-3-bromanyl-propan-1-one'>LFI</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
[[Category: Stanway, S]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bfw OCA], [https://pdbe.org/8bfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bfw RCSB], [https://www.ebi.ac.uk/pdbsum/8bfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bfw ProSAT]</span></td></tr>
[[Category: Hyvonen, M]]
</table>
[[Category: Bezerra, G]]
== Function ==
[[Category: Demydchuk, Y]]
[https://www.uniprot.org/uniprot/ACE2_HUMAN ACE2_HUMAN] Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses.<ref>PMID:10969042</ref> <ref>PMID:10924499</ref> <ref>PMID:14647384</ref>
[[Category: Harman, M]]
== References ==
[[Category: Brear, P]]
<references/>
[[Category: Lulla, A]]
__TOC__
[[Category: Chen, L]]
</StructureSection>
[[Category: Dods, R]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Bezerra G]]
[[Category: Brear P]]
[[Category: Chen L]]
[[Category: Demydchuk Y]]
[[Category: Dods R]]
[[Category: Harman M]]
[[Category: Hyvonen M]]
[[Category: Lulla A]]
[[Category: Stanway S]]

Revision as of 15:30, 4 October 2023

The structures of Ace2 in complex with bicyclic peptide inhibitorThe structures of Ace2 in complex with bicyclic peptide inhibitor

Structural highlights

8bfw is a 4 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.33Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACE2_HUMAN Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses.[1] [2] [3]

References

  1. Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, Breitbart RE, Acton S. A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res. 2000 Sep 1;87(5):E1-9. PMID:10969042
  2. Tipnis SR, Hooper NM, Hyde R, Karran E, Christie G, Turner AJ. A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J Biol Chem. 2000 Oct 27;275(43):33238-43. PMID:10924499 doi:http://dx.doi.org/10.1074/jbc.M002615200
  3. Li W, Moore MJ, Vasilieva N, Sui J, Wong SK, Berne MA, Somasundaran M, Sullivan JL, Luzuriaga K, Greenough TC, Choe H, Farzan M. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 2003 Nov 27;426(6965):450-4. PMID:14647384 doi:http://dx.doi.org/10.1038/nature02145

8bfw, resolution 2.33Å

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