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[[Image:2er9.jpg|left|200px]]
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{{STRUCTURE_2er9|  PDB=2er9  |  SCENE=  }}
'''X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES.'''


==X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES.==
<StructureSection load='2er9' size='340' side='right'caption='[[2er9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2er9]] is a 2 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=2ER9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ER9 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</scene>, <scene name='pdbligand=STA:STATINE'>STA</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=2er9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2er9 OCA], [https://pdbe.org/2er9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2er9 RCSB], [https://www.ebi.ac.uk/pdbsum/2er9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2er9 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/er/2er9_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=2er9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The conformation of a statine-containing renin inhibitor complexed with the aspartic proteinase from the fungus Endothia parasitica (EC 3.4.23.6) has been determined by X-ray diffraction at 2.2-A resolution (R = 0.17). We describe the structure of the complex at high resolution and compare this with a 3.0-A resolution analysis of a bound inhibitor, L-364,099, containing a cyclohexylalanine analogue of statine. The inhibitors bind in extended conformations in the long active-site cleft, and the hydroxyl of the transition-state analogue, statine, interacts strongly with the catalytic aspartates via hydrogen bonds to the essential carboxyl groups. This work provides a detailed structural analysis of the role of statine in peptide inhibitors. It shows conclusively that statine should be considered a dipeptide analogue (occupying P1 to P1') despite lacking the equivalent of a P1' side chain, although other inhibitor residues (especially P2) may compensate by interacting at the unoccupied S1' specificity subsite.


==Overview==
X-ray studies of aspartic proteinase-statine inhibitor complexes.,Cooper JB, Foundling SI, Blundell TL, Boger J, Jupp RA, Kay J Biochemistry. 1989 Oct 17;28(21):8596-603. PMID:2690945<ref>PMID:2690945</ref>
The conformation of a statine-containing renin inhibitor complexed with the aspartic proteinase from the fungus Endothia parasitica (EC 3.4.23.6) has been determined by X-ray diffraction at 2.2-A resolution (R = 0.17). We describe the structure of the complex at high resolution and compare this with a 3.0-A resolution analysis of a bound inhibitor, L-364,099, containing a cyclohexylalanine analogue of statine. The inhibitors bind in extended conformations in the long active-site cleft, and the hydroxyl of the transition-state analogue, statine, interacts strongly with the catalytic aspartates via hydrogen bonds to the essential carboxyl groups. This work provides a detailed structural analysis of the role of statine in peptide inhibitors. It shows conclusively that statine should be considered a dipeptide analogue (occupying P1 to P1') despite lacking the equivalent of a P1' side chain, although other inhibitor residues (especially P2) may compensate by interacting at the unoccupied S1' specificity subsite.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2ER9 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ER9 OCA].
</div>
<div class="pdbe-citations 2er9" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
X-ray studies of aspartic proteinase-statine inhibitor complexes., Cooper JB, Foundling SI, Blundell TL, Boger J, Jupp RA, Kay J, Biochemistry. 1989 Oct 17;28(21):8596-603. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2690945 2690945]
*[[Pepsin|Pepsin]]
[[Category: Hydrolase]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
[[Category: Single protein]]
== References ==
[[Category: Blundell, T L.]]
<references/>
[[Category: Boger, J.]]
__TOC__
[[Category: Cooper, J B.]]
</StructureSection>
[[Category: Foundling, S I.]]
[[Category: Cryphonectria parasitica]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:01:45 2008''
[[Category: Large Structures]]
[[Category: Blundell TL]]
[[Category: Boger J]]
[[Category: Cooper JB]]
[[Category: Foundling SI]]
Retrieved from "https://proteopedia.org/2er9"