1epp: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1epp.gif|left|200px]]<br /><applet load="1epp" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1epp, resolution 1.9&Aring;" />
-'''ANALYSES OF LIGAND BINDING IN FIVE ENDOTHIAPEPSIN CRYSTAL COMPLEXES AND THEIR USE IN THE DESIGN AND EVALUATION OF NOVEL RENIN INHIBITORS'''<br />
-==Overview==
+==ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH PD-130,693 (MAS PHE LYS+MTF STA MBA)==
+<StructureSection load='1epp' size='340' side='right'caption='[[1epp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1epp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EPP 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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1Z1:N-(DIMETHYLSULFAMOYL)-L-PHENYLALANYL-N-[(1S,2S)-2-HYDROXY-4-{[(2S)-2-METHYLBUTYL]AMINO}-1-(2-METHYLPROPYL)-4-OXOBUTYL]-N~6~-(METHYLCARBAMOTHIOYL)-L-LYSINAMIDE'>1Z1</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=1epp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epp OCA], [https://pdbe.org/1epp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1epp RCSB], [https://www.ebi.ac.uk/pdbsum/1epp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1epp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CARP_CRYPA CARP_CRYPA]
+== 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/ep/1epp_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=1epp ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
 Five renin inhibitors were cocrystallized with endothiapepsin, a fungal enzyme homologous to renin. Crystal structures of inhibitor-bound complexes have provided invaluable insight regarding the three-dimensional structure of the aspartic proteinase family of enzymes, as well as the steric and polar interactions that occur between the proteins and the bound ligands. Beyond this, subtleties of binding have been revealed, including multiple subsite binding modes and subsite interdependencies. This information has been applied in the design of novel potent renin inhibitors and in the understanding of structure-activity relationships and enzyme selectivities.
-==About this Structure==
+Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors.,Lunney EA, Hamilton HW, Hodges JC, Kaltenbronn JS, Repine JT, Badasso M, Cooper JB, Dealwis C, Wallace BA, Lowther WT, et al. J Med Chem. 1993 Nov 26;36(24):3809-20. PMID:8254610<ref>PMID:8254610</ref>
-EPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MAS:'>MAS</scene> and <scene name='pdbligand=MTF:'>MTF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPP OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors., Lunney EA, Hamilton HW, Hodges JC, Kaltenbronn JS, Repine JT, Badasso M, Cooper JB, Dealwis C, Wallace BA, Lowther WT, et al., J Med Chem. 1993 Nov 26;36(24):3809-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8254610 8254610]
+</div>
-[[Category: Endothiapepsin]]
+<div class="pdbe-citations 1epp" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
-[[Category: Blundell, T L.]]
-[[Category: Cooper, J B.]]
-[[Category: Wallace, B A.]]
-[[Category: MAS]]
-[[Category: MTF]]
-[[Category: SO4]]
-[[Category: hydrolase(acid proteinase)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:17 2008''
+==See Also==
+*[[Pepsin|Pepsin]]
+*[[Proteinase 3D structures|Proteinase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Cryphonectria parasitica]]
+[[Category: Large Structures]]
+[[Category: Blundell TL]]
+[[Category: Cooper JB]]
+[[Category: Wallace BA]]