Protein-phospholipid interactions in blood clotting.
Most steps of the blood clotting cascade require the assembly of a serine protease with its specific regulatory protein on a suitable phospholipid bilayer. Unfortunately, the molecular details of how blood clotting proteins bind to membrane surfaces remain poorly understood, owing to a dearth of techniques for studying protein-membrane interactions at high resolution. Our laboratories are tackling this question using a combination of approaches, including nanoscale membrane bilayers, solid-state NMR, and large-scale molecular dynamics simulations. These studies are now providing structural insights at atomic resolution into clotting protein-membrane interactions.
Department of Biochemistry, College of Medicine, University of Illinois at Urbana-Champaign, 506 S. Mathews Ave., Urbana, IL, USA. jhmorris@illinois.edu
James H
JH
Morrissey
Rebecca L
RL
Davis-Harrison
Narjes
N
Tavoosi
Ke
K
Ke
Vincent
V
Pureza
John M
JM
Boettcher
Mary C
MC
Clay
Chad M
CM
Rienstra
Y Zenmei
YZ
Ohkubo
Taras V
TV
Pogorelov
Emad
E
Tajkhorshid
D000465:Algorithms; D001777:Blood Coagulation; D002462:Cell Membrane / Q000378:metabolism; D003198:Computer Simulation; D015942:Factor VIIa / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008954:Models, Biological; D036103:Nanotechnology / Q000379:methods; D010743:Phospholipids / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D057057:Serine Proteases / Q000737:chemistry; D013925:Thromboplastin / Q000378:metabolism
D010743:Phospholipids; D011506:Proteins; D013925:Thromboplastin; D057057:Serine Proteases; D015942:Factor VIIa