Literature summary for 3.4.21.5 extracted from

Malovichko, M.; Sabo, T.; Maurer, M.
Ligand binding to anion-binding exosites regulates conformational properties of thrombin (2013), J. Biol. Chem., 288, 8667-8678.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00734	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
protease-activated receptor 3 residues 44-56 + H2O	-	Homo sapiens	?	-	?

General Information

General Information	Comment	Organism
physiological function	thrombin is regulated via the extended active site region and anion-binding exosites I and II. Protease-activated receptor 3 residues 44-56 and protease-activated receptor 1 residues 49-62 bind to thrombin anion-binding exosite I and exhibit long range effects over to anion-binding exosite II. Hirudin residues 54-65 focus more on anion-binding exosite I and do not transmit influences over to anion-binding exosite II. D-Phe-Pro-Arg-chloromethyl ketone inhibition at the thrombin active site leads to further local and long range consequences to thrombin-anion-binding exosite I ligand complexes with the autolysis loop often most affected	Homo sapiens

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Release 2023.1 (January 2023)