This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


User:Cody Couperus/Sandbox 1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 57: Line 57:
==Thrombin Allostery==
==Thrombin Allostery==
-
Binding of thrombin by sodium or at exosite I stabilizes a form of thrombin that improves substrate recognition. This occurs due to energetic linkage between these sites to the S1 binding pocket and oxanion hole. Rapid kinetic analysis suggests that thrombin is in a dynamic equilibrium that consists of a fast, slow, and inactive state. There is question as to the physiologic relevance of the inactive state. Regardless, there will be a proportion of fast:slow thrombin and sodium binding to the fast form stabilizes that conformation. Indeed, mutation of the residues involved in sodium binding diminishes the activity of thrombin. It should be restated, that current data suggest that sodium binding does not induce a conformation change, rather, it stabilizes a conformation of thrombin that has greater activity.
+
Binding of thrombin by sodium or at exosite I stabilizes a form of thrombin that improves substrate recognition.<ref>PMID: 22944689</ref> This occurs due to energetic linkage between these sites to the S1 binding pocket and oxanion hole. Rapid kinetic analysis suggests that thrombin is in a dynamic equilibrium that consists of a fast, slow, and inactive state<ref>PMID: 22944689</ref>. There is question as to the physiologic relevance of the inactive state. Regardless, there will be a proportion of fast:slow thrombin and sodium binding to the fast form stabilizes that conformation. Indeed, mutation of the residues involved in sodium binding diminishes the activity of thrombin.<ref>PMID: 22944689</ref> It should be restated, that current data suggest that sodium binding does not induce a conformation change, rather, it stabilizes a conformation of thrombin that has greater activity.

Revision as of 14:40, 28 April 2014

Thrombin: Structure and Function

Thrombin (1PPB) viewed in cartoon representation colored by secondary structure. Active site residues Ser195, Asp102, and His57 are viewed in ball and stick form.

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Cody Couperus

Retrieved from "http://52.214.119.220/wiki/index.php/User:Cody_Couperus/Sandbox_1"
Personal tools