1dva: Difference between revisions

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[[Image:1dva.~~gif~~|left|200px]]

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

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~~'''~~CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE PEPTIDE EXOSITE INHIBITOR E-76 AND COAGULATION FACTOR VIIA~~'''~~

===CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE PEPTIDE EXOSITE INHIBITOR E-76 AND COAGULATION FACTOR VIIA===

~~==Overview==~~

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~~Potent anticoagulants have been derived by targeting the tissue factor-factor VIIa complex with naive peptide libraries displayed on M13 phage.~~ The ~~peptides specifically block~~ the ~~activation of factor X with a median inhibitory concentration of 1 nM and selectively inhibit tissue-factor-dependent clotting. The peptides do not bind~~ to the ~~active site of factor VIIa; rather, they work by binding to an exosite~~ on ~~the factor VIIa protease domain, and non-competitively inhibit activation of factor X and amidolytic activity~~. ~~One such peptide (E-76~~) ~~has a well defined structure in solution determined by NMR spectroscopy that~~ is ~~similar to~~ the X-ray crystal structure when complexed with factor VIIa. These structural and functional studies indicate an allosteric 'switch' mechanism of inhibition involving an activation loop of factor VIIa and represent a new framework for developing inhibitors of serine proteases.

The line below this paragraph, {{ABSTRACT_PUBMED_10761907}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10761907 is the PubMed ID number.

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==About this Structure==

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[[Category: Ultsch, M H.]]

[[Category: Protein-peptide complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 14~~:19:23 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:40:17 2008''

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-[[Image:1dva.gif|left|200px]]
+{{Seed}}
+[[Image:1dva.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dva|  PDB=1dva  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE PEPTIDE EXOSITE INHIBITOR E-76 AND COAGULATION FACTOR VIIA'''
+===CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE PEPTIDE EXOSITE INHIBITOR E-76 AND COAGULATION FACTOR VIIA===
-==Overview==
+<!--
-Potent anticoagulants have been derived by targeting the tissue factor-factor VIIa complex with naive peptide libraries displayed on M13 phage. The peptides specifically block the activation of factor X with a median inhibitory concentration of 1 nM and selectively inhibit tissue-factor-dependent clotting. The peptides do not bind to the active site of factor VIIa; rather, they work by binding to an exosite on the factor VIIa protease domain, and non-competitively inhibit activation of factor X and amidolytic activity. One such peptide (E-76) has a well defined structure in solution determined by NMR spectroscopy that is similar to the X-ray crystal structure when complexed with factor VIIa. These structural and functional studies indicate an allosteric 'switch' mechanism of inhibition involving an activation loop of factor VIIa and represent a new framework for developing inhibitors of serine proteases.
+The line below this paragraph, {{ABSTRACT_PUBMED_10761907}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10761907 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10761907}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Ultsch, M H.]]
 [[Category: Protein-peptide complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:19:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:40:17 2008''