2c4f: Difference between revisions

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==Overview==

The activated factor VII/tissue factor complex (FVIIa/TF) is known to play, a key role in the formation of blood clots. Inhibition of this complex may, lead to new antithrombotic drugs. A fluoropyridine-based series of, FVIIa/TF inhibitors was discovered which utilized a diisopropylamino group, for binding in the S2 and S3 binding pockets of the active site of the, enzyme complex. In this series, an enhancement in binding affinity was, observed by substitution at the 5-position of the hydroxybenzoic acid, sidechain. An X-ray crystal structure indicates that amides at this, position may increase inhibitor binding affinity through interactions with, the S1'/S2' pocket.

The activated factor VII/tissue factor complex (FVIIa/TF) is known to play a key role in the formation of blood clots. Inhibition of this complex may lead to new antithrombotic drugs. A fluoropyridine-based series of FVIIa/TF inhibitors was discovered which utilized a diisopropylamino group for binding in the S2 and S3 binding pockets of the active site of the enzyme complex. In this series, an enhancement in binding affinity was observed by substitution at the 5-position of the hydroxybenzoic acid sidechain. An X-ray crystal structure indicates that amides at this position may increase inhibitor binding affinity through interactions with the S1'/S2' pocket.

==Disease==

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[[Category: Coagulation factor VIIa]]

[[Category: Protein complex]]

[[Category: Kohrt, J.T.]]

[[Category: Kohrt, J T.]]

[[Category: Zhang, E.]]

[[Category: CA]]

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[[Category: transmembrane]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:45 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The activated factor VII/tissue factor complex (FVIIa/TF) is known to play, a key role in the formation of blood clots. Inhibition of this complex may, lead to new antithrombotic drugs. A fluoropyridine-based series of, FVIIa/TF inhibitors was discovered which utilized a diisopropylamino group, for binding in the S2 and S3 binding pockets of the active site of the, enzyme complex. In this series, an enhancement in binding affinity was, observed by substitution at the 5-position of the hydroxybenzoic acid, sidechain. An X-ray crystal structure indicates that amides at this, position may increase inhibitor binding affinity through interactions with, the S1'/S2' pocket.
+The activated factor VII/tissue factor complex (FVIIa/TF) is known to play a key role in the formation of blood clots. Inhibition of this complex may lead to new antithrombotic drugs. A fluoropyridine-based series of FVIIa/TF inhibitors was discovered which utilized a diisopropylamino group for binding in the S2 and S3 binding pockets of the active site of the enzyme complex. In this series, an enhancement in binding affinity was observed by substitution at the 5-position of the hydroxybenzoic acid sidechain. An X-ray crystal structure indicates that amides at this position may increase inhibitor binding affinity through interactions with the S1'/S2' pocket.
 ==Disease==
@@ Line 16: / Line 16: @@
 [[Category: Coagulation factor VIIa]]
 [[Category: Protein complex]]
-[[Category: Kohrt, J.T.]]
+[[Category: Kohrt, J T.]]
 [[Category: Zhang, E.]]
 [[Category: CA]]
@@ Line 37: / Line 37: @@
 [[Category: transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:31:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:45 2008''