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1er8

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(New page: 200px<br /><applet load="1er8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1er8, resolution 2.0&Aring;" /> '''THE ACTIVE SITE OF AS...)
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[[Image:1er8.gif|left|200px]]<br /><applet load="1er8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1er8, resolution 2.0&Aring;" />
 
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'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''<br />
 
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==Overview==
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==THE ACTIVE SITE OF ASPARTIC PROTEINASES==
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The active site of the aspartic proteinase, endothiapepsin, has been, defined by X-ray analysis and restrained least-squares refinement at 2.1 A, resolution with a crystallographic agreement value of 0.16. The, environments of the two catalytically important aspartyl groups are, remarkably similar and the contributions of the NH2- and COOH-terminal, domains to the catalytic centre are related by a local 2-fold axis. The, carboxylates of the aspartyls share a hydrogen bond and have equivalent, contacts to a bound water molecule or hydroxonium ion lying on the local, diad. The main chains around 32 and 215 are connected by a novel, interaction involving diad-related threonines. It is suggested that the, two pKa values of the active site aspartyls arise from a structure not, unlike that in maleic acid with a hydrogen-bonded intermediate species and, a dicarboxylate characterised by electrostatic repulsions between the two, negatively charged groups.
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<StructureSection load='1er8' size='340' side='right'caption='[[1er8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1er8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica] and [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ER8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ER8 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]] 2&#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=DHI:D-HISTIDINE'>DHI</scene></td></tr>
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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=1er8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1er8 OCA], [https://pdbe.org/1er8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1er8 RCSB], [https://www.ebi.ac.uk/pdbsum/1er8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1er8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ANGT_HORSE ANGT_HORSE] Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.[UniProtKB:P01019] Acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone. Acts by binding to angiotensin receptors AGTR1 and AGTR2. Also binds the DEAR/FBXW7-AS1 receptor.[UniProtKB:P01015][UniProtKB:P01019] Stimulates aldosterone release.[UniProtKB:P01019] Is a ligand for the G-protein coupled receptor MAS1. Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets.[UniProtKB:P11859]
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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/er/1er8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1er8 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ER8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ER8 OCA].
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*[[Pepsin|Pepsin]]
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__TOC__
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==Reference==
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</StructureSection>
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The active site of aspartic proteinases., Pearl L, Blundell T, FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=6381096 6381096]
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[[Category: Cryphonectria parasitica]]
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[[Category: Hydrolase]]
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[[Category: Equus caballus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blundell, T.L.]]
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[[Category: Blundell TL]]
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[[Category: Cooper, J.B.]]
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[[Category: Cooper JB]]
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[[Category: Hemmings, A.M.]]
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[[Category: Hemmings AM]]
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[[Category: Szelke, M.]]
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[[Category: Szelke M]]
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[[Category: Veerapandian, B.]]
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[[Category: Veerapandian B]]
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[[Category: hydrolase (acid proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:14:33 2007''
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Current revision

THE ACTIVE SITE OF ASPARTIC PROTEINASES

PDB ID 1er8

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