2er0
From Proteopedia
(New page: 200px<br /><applet load="2er0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2er0, resolution 3.0Å" /> '''X-RAY STUDIES OF ASPA...) |
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| - | [[Image:2er0.jpg|left|200px]]<br /><applet load="2er0" size=" | + | [[Image:2er0.jpg|left|200px]]<br /><applet load="2er0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2er0, resolution 3.0Å" /> | caption="2er0, resolution 3.0Å" /> | ||
'''X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES'''<br /> | '''X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The conformation of a statine-containing renin inhibitor complexed with | + | 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== | ==About this Structure== | ||
| - | 2ER0 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/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http:// | + | 2ER0 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/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ER0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blundell, T | + | [[Category: Blundell, T L.]] |
[[Category: Boger, J.]] | [[Category: Boger, J.]] | ||
| - | [[Category: Cooper, J | + | [[Category: Cooper, J B.]] |
| - | [[Category: Foundling, S | + | [[Category: Foundling, S I.]] |
[[Category: hydrolase (acid proteinase)]] | [[Category: hydrolase (acid proteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:43 2008'' |
Revision as of 15:13, 21 February 2008
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X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES
Overview
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
2ER0 is a Single protein structure of sequence from [1]. Active as Hydrolase, with EC number 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 Full crystallographic information is available from OCA.
Reference
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
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