1r4l

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[[Image:1r4l.png|left|200px]]
 
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==Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)==
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The line below this paragraph, containing "STRUCTURE_1r4l", creates the "Structure Box" on the page.
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<StructureSection load='1r4l' size='340' side='right'caption='[[1r4l]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1r4l]] is a 5 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=1R4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4L FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XX5:(S,S)-2-{1-CARBOXY-2-[3-(3,5-DICHLORO-BENZYL)-3H-IMIDAZOL-4-YL]-ETHYLAMINO}-4-METHYL-PENTANOIC+ACID'>XX5</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1r4l| PDB=1r4l | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4l OCA], [https://pdbe.org/1r4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4l RCSB], [https://www.ebi.ac.uk/pdbsum/1r4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/1r4l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r4l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence. ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS). To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively. Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis. The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino] -4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity. A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
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===Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)===
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ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.,Towler P, Staker B, Prasad SG, Menon S, Tang J, Parsons T, Ryan D, Fisher M, Williams D, Dales NA, Patane MA, Pantoliano MW J Biol Chem. 2004 Apr 23;279(17):17996-8007. Epub 2004 Jan 30. PMID:14754895<ref>PMID:14754895</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1r4l" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_14754895}}, adds the Publication Abstract to the page
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*[[Angiotensin-Converting Enzyme 3D structures|Angiotensin-Converting Enzyme 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 14754895 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14754895}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1r4l]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4L OCA].
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==Reference==
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<ref group="xtra">PMID:014754895</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Dales, N A.]]
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[[Category: Large Structures]]
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[[Category: Fisher, M.]]
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[[Category: Dales NA]]
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[[Category: Menon, S.]]
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[[Category: Fisher M]]
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[[Category: Pantoliano, M W.]]
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[[Category: Menon S]]
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[[Category: Parsons, T.]]
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[[Category: Pantoliano MW]]
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[[Category: Patane, M A.]]
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[[Category: Parsons T]]
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[[Category: Prasad, S G.]]
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[[Category: Patane MA]]
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[[Category: Ryan, D.]]
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[[Category: Prasad SG]]
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[[Category: Staker, B.]]
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[[Category: Ryan D]]
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[[Category: Tang, J.]]
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[[Category: Staker B]]
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[[Category: Towler, P.]]
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[[Category: Tang J]]
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[[Category: Williams, D.]]
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[[Category: Towler P]]
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[[Category: Chloride ion binding site]]
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[[Category: Williams D]]
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[[Category: Collectrin homology domain]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor bound conformation]]
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[[Category: Zinc ion binding site]]
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[[Category: Zinc metallopeptidase domain]]
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Current revision

Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)

PDB ID 1r4l

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