This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1eed

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1eed" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eed, resolution 2.0&Aring;" /> '''X-RAY CRYSTALLOGRAPHI...)
Current revision (10:01, 20 March 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1eed.gif|left|200px]]<br /><applet load="1eed" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1eed, resolution 2.0&Aring;" />
 
-
'''X-RAY CRYSTALLOGRAPHIC ANALYSIS OF INHIBITION OF ENDOTHIAPEPSIN BY CYCLOHEXYL RENIN INHIBITORS'''<br />
 
-
==Overview==
+
==X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors==
-
The crystal structures of endothiapepsin, a fungal aspartic proteinase (EC, 3.4.23.6), cocrystallized with two oligopeptide renin inhibitors, PD125967, and PD125754, have been determined at 2.0-A resolution and refined to, R-factors of 0.143 and 0.153, respectively. These inhibitors, which are of, the hydroxyethylene and statine types, respectively, possess a, cyclohexylalanine side chain at P1 and have interesting functionalities at, the P3 position which, until now, have not been subjected to, crystallographic analysis. PD125967 has a bis(1-naphthylmethyl)acetyl, residue at P3, and PD125754 possesses a hydroxyethylene analogue of the, P3-P2 peptide bond for proteolytic stability. The structures reveal that, the S3 pocket accommodates one naphthyl ring with conformational changes, of the Asp 77 and Asp 114 side chains, the other naphthyl group residing, in the S4 region. The P3-P2 hydroxyethylene analogue of PD125754 forms a, hydrogen bond with the NH of Thr 219, thereby making the same interaction, with the enzyme as the equivalent peptide groups of all inhibitors studied, so far. The absence of side chains at the P2 and P1' positions of this, inhibitor allows water molecules to occupy the respective pockets in the, complex. The relative potencies of PD125967 and PD125754 for, endothiapepsin are consistent with the changes in solvent-accessible area, which take place on inhibitor binding.
+
<StructureSection load='1eed' size='340' side='right'caption='[[1eed]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1eed]] 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=1EED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EED 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&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0EO:(2S)-2-[[(3S,4S)-5-CYCLOHEXYL-4-[[(4S,5S)-5-[(2-METHYLPROPAN-2-YL)OXYCARBONYLAMINO]-4-OXIDANYL-6-PHENYL-HEXANOYL]AMINO]-3-OXIDANYL-PENTANOYL]AMINO]-4-METHYL-PENTANOIC+ACID'>0EO</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=1eed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eed OCA], [https://pdbe.org/1eed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eed RCSB], [https://www.ebi.ac.uk/pdbsum/1eed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eed 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/ee/1eed_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=1eed ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1EED is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EED OCA].
+
*[[Pepsin|Pepsin]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors., Cooper J, Quail W, Frazao C, Foundling SI, Blundell TL, Humblet C, Lunney EA, Lowther WT, Dunn BM, Biochemistry. 1992 Sep 8;31(35):8142-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1525155 1525155]
+
[[Category: Cryphonectria parasitica]]
-
[[Category: Endothiapepsin]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Blundell TL]]
-
[[Category: Blundell, T.L.]]
+
[[Category: Cooper JB]]
-
[[Category: Cooper, J.B.]]
+
[[Category: Frazao C]]
-
[[Category: Frazao, C.]]
+
-
[[Category: aspartic proteinase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:56:30 2007''
+

Current revision

X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors

PDB ID 1eed

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eed"
Personal tools