Blood clotting protein binding to a membrane

Computer simulation of how a blood clotting protein interacts with a membrane surface. This is from a molecular dynamics simulation of the GLA domain of human coagulation factor VIIa interacting with a membrane bilayer consisting of phosphatidylserine (see Ohkubo & Tajkhorshid (2008) Structure 16:72-81). Factor VIIa is the enzyme that triggers blood clotting, and its GLA domain shown here is the part of the protein that allows it to bind to membranes. The red spheres are calcium ions tightly bound within the GLA domain. Note how the GLA domain initially encounters the membrane surface, then eventually embeds part of itself into the membrane. This detailed computer simulation and others like it from the Tajkhorshid lab at the University of Illinois have provided important new insights into how blood clotting proteins function in normal hemostasis and thrombotic disease. More recently, a study from three labs at the Univ. of Illinois has now shown that GLA domains bind to membranes via a combination of "phospho-L-serine-specific" and "phosphate-specific" interactions (see Tavoosi et al. (2011) J. Biol. Chem., in press). Video uploaded with permission from Zenmei Ohkubo & Emad Tajkhorshid.
http://www.sciencedirect.com/science/article/pii/S0969212607004662
http://dx.doi.org/10.1074/jbc.M111.251769

Category:

Science & Technology

Tags:

• blood clotting
• membranes
• phosphatidylserine
• factor VIIa
• molecular dynamics
• simulation
• hemostasis

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