1o6x: Difference between revisions

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-[[Image:1o6x.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1o6x", creates the "Structure Box" on the page.
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-{{STRUCTURE_1o6x|  PDB=1o6x  |  SCENE=  }}
-'''NMR SOLUTION STRUCTURE OF THE ACTIVATION DOMAIN OF HUMAN PROCARBOXYPEPTIDASE A2'''
+==NMR solution structure of the activation domain of human procarboxypeptidase A2==
+<StructureSection load='1o6x' size='340' side='right'caption='[[1o6x]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1o6x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6X FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1o6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6x OCA], [https://pdbe.org/1o6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6x RCSB], [https://www.ebi.ac.uk/pdbsum/1o6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6x 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/o6/1o6x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1o6x ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The activation domain of human procarboxypeptidase A2, ADA2h, is an 81-residue globular domain released during the proteolytic activation of the proenzyme. The role of this and other similar domains as assistants of the correct folding of the enzyme is not fully understood. The folding pathway of ADA2h was characterized previously, and it was also observed that under certain conditions it may convert into amyloid fibrils in vitro. To gain insight into these processes, a detailed description of its three-dimensional structure in aqueous solution is required so that eventual changes could be properly monitored. A complete assignment of the (1)H and (15)N resonances of ADA2h was performed, and the solution structure, as derived from a set of 1688 nonredundant constraints, is very well defined (pairwise backbone RMSD = 0.67 +/- 0.17 A for residues 10-80). The structure is composed of two antiparallel alpha-helices comprising residues 19-32 and 58-69 packed on the same side of a three-stranded beta-sheet spanning residues 10-15, 50-55, and 73-75. The global fold for the isolated human A2 activation domain is very similar to that of porcine carboxypeptidase B, as well as to the structure of the domain in the crystal of the intact human proenzyme. The observed structural differences relative to the intact human proenzyme are located at the interface between the activation domain and the enzyme and can be related with the activation mechanism. The backbone amide proton exchange behavior of ADA2h was also examined. The global free energy of unfolding obtained from exchange data of the most protected amide protons at pH 7.0 and 298K is 4.9 +/- 0.3 kcal.mole(-1), in good agreement with the values determined by thermal or denaturant unfolding studies.
-==Overview==
+NMR solution structure of the activation domain of human procarboxypeptidase A2.,Jimenez MA, Villegas V, Santoro J, Serrano L, Vendrell J, Aviles FX, Rico M Protein Sci. 2003 Feb;12(2):296-305. PMID:12538893<ref>PMID:12538893</ref>
-The activation domain of human procarboxypeptidase A2, ADA2h, is an 81-residue globular domain released during the proteolytic activation of the proenzyme. The role of this and other similar domains as assistants of the correct folding of the enzyme is not fully understood. The folding pathway of ADA2h was characterized previously, and it was also observed that under certain conditions it may convert into amyloid fibrils in vitro. To gain insight into these processes, a detailed description of its three-dimensional structure in aqueous solution is required so that eventual changes could be properly monitored. A complete assignment of the (1)H and (15)N resonances of ADA2h was performed, and the solution structure, as derived from a set of 1688 nonredundant constraints, is very well defined (pairwise backbone RMSD = 0.67 +/- 0.17 A for residues 10-80). The structure is composed of two antiparallel alpha-helices comprising residues 19-32 and 58-69 packed on the same side of a three-stranded beta-sheet spanning residues 10-15, 50-55, and 73-75. The global fold for the isolated human A2 activation domain is very similar to that of porcine carboxypeptidase B, as well as to the structure of the domain in the crystal of the intact human proenzyme. The observed structural differences relative to the intact human proenzyme are located at the interface between the activation domain and the enzyme and can be related with the activation mechanism. The backbone amide proton exchange behavior of ADA2h was also examined. The global free energy of unfolding obtained from exchange data of the most protected amide protons at pH 7.0 and 298K is 4.9 +/- 0.3 kcal.mole(-1), in good agreement with the values determined by thermal or denaturant unfolding studies.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-O6X 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=1O6X OCA].
+</div>
+<div class="pdbe-citations 1o6x" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-NMR solution structure of the activation domain of human procarboxypeptidase A2., Jimenez MA, Villegas V, Santoro J, Serrano L, Vendrell J, Aviles FX, Rico M, Protein Sci. 2003 Feb;12(2):296-305. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12538893 12538893]
+*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
-[[Category: Carboxypeptidase A2]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Aviles, F X.]]
+[[Category: Aviles FX]]
-[[Category: Jimenez, M A.]]
+[[Category: Jimenez MA]]
-[[Category: Rico, M.]]
+[[Category: Rico M]]
-[[Category: Santoro, J.]]
+[[Category: Santoro J]]
-[[Category: Serrano, L.]]
+[[Category: Serrano L]]
-[[Category: Vendrell, J.]]
+[[Category: Vendrell J]]
-[[Category: Villegas, V.]]
+[[Category: Villegas V]]
-[[Category: Activation domain]]
-[[Category: Carboxypeptidase]]
-[[Category: Hydrolase]]
-[[Category: Metalloprote]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:27:37 2008''