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1aye

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{{Seed}}
 
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[[Image:1aye.png|left|200px]]
 
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==HUMAN PROCARBOXYPEPTIDASE A2==
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The line below this paragraph, containing "STRUCTURE_1aye", creates the "Structure Box" on the page.
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<StructureSection load='1aye' size='340' side='right'caption='[[1aye]], [[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'>[[1aye]] is a 1 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=1AYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AYE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#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=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1aye| PDB=1aye | 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=1aye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aye OCA], [https://pdbe.org/1aye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aye RCSB], [https://www.ebi.ac.uk/pdbsum/1aye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aye ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CBPA2_HUMAN CBPA2_HUMAN]
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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/ay/1aye_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=1aye 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 three-dimensional structure of human procarboxypeptidase A2 has been determined using X-ray crystallography at 1.8 A resolution. This is the first detailed structural report of a human pancreatic carboxypeptidase and of its zymogen. Human procarboxypeptidase A2 is formed by a pro-segment of 96 residues, which inhibits the enzyme, and a carboxypeptidase moiety of 305 residues. The pro-enzyme maintains the general fold when compared with other non-human counterparts. The globular part of the pro-segment docks into the enzyme moiety and shields the S2-S4 substrate binding sites, promoting inhibition. Interestingly, important differences are found in the pro-segment which allow the identification of the structural determinants of the diverse activation behaviours of procarboxypeptidases A1, B and A2, particularly of the latter. The benzylsuccinic inhibitor is able to diffuse into the active site of procarboxypeptidase A2 in the crystals. The structure of the zymogen-inhibitor complex has been solved at 2.2 A resolution. The inhibitor enters the active site through a channel formed at the interface between the pro-segment and the enzyme regions and interacts with important elements of the active site. The derived structural features explain the intrinsic activity of A1/A2 pro-enzymes for small substrates.
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===HUMAN PROCARBOXYPEPTIDASE A2===
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The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen.,Garcia-Saez I, Reverter D, Vendrell J, Aviles FX, Coll M EMBO J. 1997 Dec 1;16(23):6906-13. PMID:9384570<ref>PMID:9384570</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 1aye" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9384570}}, adds the Publication Abstract to the page
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9384570 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9384570}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1AYE is a 1 chain structure of 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=1AYE OCA].
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==Reference==
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<ref group="xtra">PMID:9384570</ref><references group="xtra"/>
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[[Category: Carboxypeptidase A2]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Aviles, F X.]]
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[[Category: Large Structures]]
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[[Category: Coll, M.]]
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[[Category: Aviles FX]]
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[[Category: Garcia-Saez, I.]]
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[[Category: Coll M]]
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[[Category: Reverte, D.]]
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[[Category: Garcia-Saez I]]
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[[Category: Vendrell, J.]]
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[[Category: Reverte D]]
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[[Category: Hydrolase]]
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[[Category: Vendrell J]]
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[[Category: Serine protease]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:27:24 2009''
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Current revision

HUMAN PROCARBOXYPEPTIDASE A2

PDB ID 1aye

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