1bil: Difference between revisions

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==Overview==

The binding modes of three peptidomimetic P2-P3 butanediamide renin, inhibitors have been determined by x-ray crystallography. The inhibitors, are bound with their backbones in an extended conformation, and their side, chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side, chain at the P2 position shows stronger hydrogen-bonding and van der Waals, interactions with renin than the His side chain, which is present in the, natural substrate. The ACHPA-gamma-lactam transition state analog has, similar interactions with renin as the dihydroxyethylene transition state, analog.

The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.

==Disease==

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[[Category: aspartic proteinase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:40 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The binding modes of three peptidomimetic P2-P3 butanediamide renin, inhibitors have been determined by x-ray crystallography. The inhibitors, are bound with their backbones in an extended conformation, and their side, chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side, chain at the P2 position shows stronger hydrogen-bonding and van der Waals, interactions with renin than the His side chain, which is present in the, natural substrate. The ACHPA-gamma-lactam transition state analog has, similar interactions with renin as the dihydroxyethylene transition state, analog.
+The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.
 ==Disease==
@@ Line 23: / Line 23: @@
 [[Category: aspartic proteinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:32:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:40 2008''