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3er5

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{{Seed}}
 
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[[Image:3er5.png|left|200px]]
 
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==THE ACTIVE SITE OF ASPARTIC PROTEINASES==
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The line below this paragraph, containing "STRUCTURE_3er5", creates the "Structure Box" on the page.
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<StructureSection load='3er5' size='340' side='right'caption='[[3er5]], [[Resolution|resolution]] 1.80&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'>[[3er5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crypa Crypa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ER5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ER5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=STA:STATINE'>STA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30] </span></td></tr>
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{{STRUCTURE_3er5| PDB=3er5 | 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=3er5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3er5 OCA], [https://pdbe.org/3er5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3er5 RCSB], [https://www.ebi.ac.uk/pdbsum/3er5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3er5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/ANGT_BOVIN ANGT_BOVIN]] Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis (By similarity). Angiotensin-2: 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 (By similarity). Angiotensin-3: stimulates aldosterone release (By similarity). Angiotensin 1-7: is a ligand for the G-protein coupled receptor MAS1 (By similarity). Has vasodilator and antidiuretic effects (By similarity). Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets (By similarity).
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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/3er5_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=3er5 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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H-189, a synthetic human renin inhibitor, and pepstatin A, a naturally occurring inhibitor of aspartic proteinases, have been co-crystallized with the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6). H-189 [Pro-His-Pro-Phe-His-Sta-(statyl)-Val-Ile-His-Lys] is an analogue of human angiotensinogen. Pepstatin A [Iva(isovaleryl)-Val-Val-Sta-Ala-Sta] is a blocked pentapeptide which inhibits many aspartic proteinases. The structures of the complexes have been determined by X-ray diffraction and refined to crystallographic R-factors of 0.15 and 0.16 at resolutions of 0.18 nm (1.8 A) and 0.2 nm (2.0 A) respectively. H-189 is in an extended conformation, in which the statine residue is a dipeptide analogue of P1 and P'1 as indicated by the conformation and network of contacts and hydrogen bonds. Pepstatin A has an extended conformation to the P'2 alanine residue, but the leucyl side chain of the terminal statine residue binds back into the S'1 subsite, and an inverse gamma-turn occurs between P'1 and P'3. The hydroxy moiety of the statine at P1 in both complexes displaces the solvent molecule that hydrogen-bonds with the catalytic aspartate residues (32 and 215) in the native enzyme. Solvent molecules originally present in the native structure at the active site are displaced on inhibitor binding (12 when pepstatin A binds; 16 when H-189 binds).
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===THE ACTIVE SITE OF ASPARTIC PROTEINASES===
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X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.,Bailey D, Cooper JB, Veerapandian B, Blundell TL, Atrash B, Jones DM, Szelke M Biochem J. 1993 Jan 15;289 ( Pt 2):363-71. PMID:8424781<ref>PMID:8424781</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 3er5" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_8424781}}, adds the Publication Abstract to the page
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*[[Pepsin|Pepsin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 8424781 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8424781}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Crypa]]
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3ER5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ER5 OCA].
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==Reference==
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X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin., Bailey D, Cooper JB, Veerapandian B, Blundell TL, Atrash B, Jones DM, Szelke M, Biochem J. 1993 Jan 15;289 ( Pt 2):363-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8424781 8424781]
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[[Category: Cryphonectria parasitica]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Bailey, D.]]
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[[Category: Bailey, D]]
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[[Category: Blundell, T L.]]
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[[Category: Blundell, T L]]
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[[Category: Cooper, J.]]
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[[Category: Cooper, J]]
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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: Acid proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:35:39 2008''
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[[Category: Hydrolase-hydrolase inhibitor]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]

Current revision

THE ACTIVE SITE OF ASPARTIC PROTEINASES

PDB ID 3er5

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