1aye: Difference between revisions

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-[[Image:1aye.gif|left|200px]]
- {{Structure
+==HUMAN PROCARBOXYPEPTIDASE A2==
-|PDB= 1aye |SIZE=350|CAPTION= <scene name='initialview01'>1aye</scene>, resolution 1.8&Aring;
+<StructureSection load='1aye' size='340' side='right'caption='[[1aye]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-|SITE= <scene name='pdbsite=1:Subsite+S1&#39;+ARG+145,+ASN+144,+TYR+248+Subsite+S1+ARG+127+...'>1</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
+<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>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Carboxypeptidase_A2 Carboxypeptidase A2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.15 3.4.17.15]
+</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>
-|GENE=
+<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>
-}}
+<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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CBPA2_HUMAN CBPA2_HUMAN]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/1aye_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''HUMAN PROCARBOXYPEPTIDASE A2'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1aye" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-AYE is a [[Single protein]] 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].
+__TOC__
+</StructureSection>
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/9384570 9384570]
-[[Category: Carboxypeptidase A2]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Aviles, F X.]]
+[[Category: Aviles FX]]
-[[Category: Coll, M.]]
+[[Category: Coll M]]
-[[Category: Garcia-Saez, I.]]
+[[Category: Garcia-Saez I]]
-[[Category: Reverte, D.]]
+[[Category: Reverte D]]
-[[Category: Vendrell, J.]]
+[[Category: Vendrell J]]
-[[Category: ZN]]
-[[Category: hydrolase]]
-[[Category: serine protease]]
-[[Category: zymogen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:11:05 2008''