1fpc: Difference between revisions

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[[Image:1fpc.~~jpg~~|left|200px]]

[[Image:1fpc.png|left|200px]]

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~~'''~~ACTIVE SITE MIMETIC INHIBITION OF THROMBIN~~'''~~

===ACTIVE SITE MIMETIC INHIBITION OF THROMBIN===

~~==Overview==~~

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~~The structures of two mimetic inhibitor complexes of human alpha~~-~~thrombin have been determined by X~~-~~ray crystallography. One mimics a beta-turn with a bicyclic ring system; the other mimics two different active-site binding modes.~~ The ~~beta-turn mimetic is used to approximate a turn found in the conformation of fibrinopeptide A~~, ~~which is catalytically released by thrombin in~~ the ~~activation of fibrinogen~~ to ~~fibrin~~. ~~The binding of the second mimetic~~ is ~~a hybrid between normal substrate and~~ the ~~abnormal binding of the potent natural leech inhibitor hirudin~~. ~~The binding of the beta~~-~~turn mimetic is tenuous, because it is like a substrate, while that of the substrate~~-~~hirudin hybrid is that of a tenacious inhibitor (which it is). Structurally retrospect modifications for rational design and improvement of both mimetic inhibitors are proposed.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15299843}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15299843 is the PubMed ID number.

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==About this Structure==

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[[Category: Mathews, I I.]]

[[Category: Tulinsky, A.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 16~~:36:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:43:52 2008''

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-[[Image:1fpc.jpg|left|200px]]
+{{Seed}}
+[[Image:1fpc.png|left|200px]]
 <!--
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 {{STRUCTURE_1fpc|  PDB=1fpc  |  SCENE=  }}
-'''ACTIVE SITE MIMETIC INHIBITION OF THROMBIN'''
+===ACTIVE SITE MIMETIC INHIBITION OF THROMBIN===
-==Overview==
+<!--
-The structures of two mimetic inhibitor complexes of human alpha-thrombin have been determined by X-ray crystallography. One mimics a beta-turn with a bicyclic ring system; the other mimics two different active-site binding modes. The beta-turn mimetic is used to approximate a turn found in the conformation of fibrinopeptide A, which is catalytically released by thrombin in the activation of fibrinogen to fibrin. The binding of the second mimetic is a hybrid between normal substrate and the abnormal binding of the potent natural leech inhibitor hirudin. The binding of the beta-turn mimetic is tenuous, because it is like a substrate, while that of the substrate-hirudin hybrid is that of a tenacious inhibitor (which it is). Structurally retrospect modifications for rational design and improvement of both mimetic inhibitors are proposed.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299843}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299843 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299843}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Mathews, I I.]]
 [[Category: Tulinsky, A.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:36:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:43:52 2008''