3GIS

Crystal Structure of Na-free Thrombin in Complex with Thrombomodulin

Summary for 3GIS

• Entry DOI: 10.2210/pdb3gis/pdb
• Descriptor: Prothrombin, Thrombomodulin, SULFATE ION, ... (6 entities in total)
• Functional Keywords: protein-protein complex, coagulation, acute phase, blood coagulation, cleavage on pair of basic residues, disease mutation, disulfide bond, gamma-carboxyglutamic acid, glycoprotein, hydrolase, kringle, protease, secreted, serine protease, zymogen, egf-like domain, hydroxylation, membrane, receptor, thrombophilia, transmembrane, blood clotting
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted, extracellular space: P00734 P00734; Membrane; Single-pass type I membrane protein: P07204
• Total number of polymer chains: 9
• Total formula weight: 146571.21

Authors

Adams, T.E.,Huntington, J.A. (deposition date: 2009-03-06, release date: 2009-08-18, Last modification date: 2024-10-30)

Primary citation

Adams, T.E.,Li, W.,Huntington, J.A.
Molecular basis of thrombomodulin activation of slow thrombin
J.Thromb.Haemost., 7:1688-1695, 2009

PubMed Abstract: Coagulation is a highly regulated process where the ability to prevent blood loss after injury is balanced against the maintenance of blood fluidity. Thrombin is at the center of this balancing act. It is the critical enzyme for producing and stabilizing a clot, but when complexed with thrombomodulin (TM) it is converted to a powerful anticoagulant. Another cofactor that may play a role in determining thrombin function is the monovalent cation Na(+). Its apparent affinity suggests that half of the thrombin generated is in a Na(+)-free 'slow' state and half is in a Na(+)-coordinated 'fast' state. While slow thrombin is a poor procoagulant enzyme, when complexed to TM it is an effective anticoagulant.

PubMed: 19656282
DOI: 10.1111/j.1538-7836.2009.03563.x

Experimental method

X-RAY DIFFRACTION (2.4 Å)