Ann Taylor Sandbox 111': Difference between revisions

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Ann Taylor

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-==Succinyl-AAPR-trypsin acyl-enzyme==
+==Serine Protease - Thrombin==
-Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction
+Thrombin is a "trypsin-like" serine protease. The Active site of thrombin is made up of a catalytic triad of Ser195, His57 and Asp102.  At the activation site, the sidechain of Asp194 makes a salt link with the N-terminus at residue 16.  Thrombin is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss.  It also converts soluble fibrinogen into insoluble strands of fibrin.  It also catalyzes many other reactions.
+The B chain consists of two domains. As is true for all of the "trypsin-like" serine proteases, each of the two thrombin domains consists mainly of a 6-stranded, antiparallel beta barrel.
+Jordan Ferguson and Shane Evans
-Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
-and display another structure.
 {{STRUCTURE_2age |  PDB=2age  |  SCENE=  }}