2er0: Difference between revisions

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[[Image:2er0.jpg|left|200px]]<br /><applet load="2er0" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2er0.jpg|left|200px]]<br /><applet load="2er0" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2er0, resolution 3.0Å" />

'''X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2ER0 OCA].

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==

Line 13:

[[Category: Hydrolase]]

[[Category: Single protein]]

[[Category: Blundell, T.L.]]

[[Category: Blundell, T L.]]

[[Category: Boger, J.]]

[[Category: Cooper, J.B.]]

[[Category: Cooper, J B.]]

[[Category: Foundling, S.I.]]

[[Category: Foundling, S I.]]

[[Category: hydrolase (acid proteinase)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 10:05:43 ~~2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:43 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2er0.jpg|left|200px]]<br /><applet load="2er0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2er0.jpg|left|200px]]<br /><applet load="2er0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2er0, resolution 3.0&Aring;" />
 '''X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES'''<br />
 ==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.
+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==
-ER0 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ER0 OCA].
+ER0 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==
@@ Line 13: / Line 13: @@
 [[Category: Hydrolase]]
 [[Category: Single protein]]
-[[Category: Blundell, T.L.]]
+[[Category: Blundell, T L.]]
 [[Category: Boger, J.]]
-[[Category: Cooper, J.B.]]
+[[Category: Cooper, J B.]]
-[[Category: Foundling, S.I.]]
+[[Category: Foundling, S I.]]
 [[Category: hydrolase (acid proteinase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:05:43 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:43 2008''