1jqp: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jqp.jpg|left|200px]]<br /><applet load="1jqp" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1jqp, resolution 2.4&Aring;" />
-'''dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family'''<br />
-==Overview==
+==dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family==
-The crystal structure of mature dipeptidyl peptidase I reveals insight, into the unique tetrameric structure, substrate binding and activation of, this atypical papain family peptidase. Each subunit is composed of three, peptides. The heavy and light chains form the catalytic domain, which, adopts the papain fold. The residual pro-part forms a beta-barrel with the, carboxylate group of Asp1 pointing towards the substrate amino-terminus., The tetrameric structure appears to stabilize the association of the two, domains and encloses a 12700 A3 spherical cavity. The tetramer contains, six chloride ions, one buried in each S2 pocket and two at subunit, interfaces.
+<StructureSection load='1jqp' size='340' side='right'caption='[[1jqp]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1jqp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQP FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1jqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jqp OCA], [https://pdbe.org/1jqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jqp RCSB], [https://www.ebi.ac.uk/pdbsum/1jqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jqp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CATC_RAT CATC_RAT] Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase (By similarity).
+== 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/jq/1jqp_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=1jqp ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-JQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAG, CL and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JQP OCA].
+*[[Cathepsin 3D structures|Cathepsin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain., Olsen JG, Kadziola A, Lauritzen C, Pedersen J, Larsen S, Dahl SW, FEBS Lett. 2001 Oct 12;506(3):201-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11602245 11602245]
+[[Category: Large Structures]]
-[[Category: Dipeptidyl-peptidase I]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Dahl SW]]
-[[Category: Dahl, S.W.]]
+[[Category: Kadziola A]]
-[[Category: Kadziola, A.]]
+[[Category: Larsen S]]
-[[Category: Larsen, S.]]
+[[Category: Lauritzen C]]
-[[Category: Lauritzen, C.]]
+[[Category: Olsen JG]]
-[[Category: Olsen, J.G.]]
+[[Category: Pedersen J]]
-[[Category: Pedersen, J.]]
-[[Category: CL]]
-[[Category: NAG]]
-[[Category: SO4]]
-[[Category: cathepsin c]]
-[[Category: chloride]]
-[[Category: cysteine protease]]
-[[Category: dpp i]]
-[[Category: papain]]
-[[Category: tetramer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:29:30 2007''