Protein-Phospholipid interactions in blood clotting

Abstract 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 dear...

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Bibliographic Details
Published inThrombosis research Vol. 125; pp. S23 - S25
Main Authors Morrissey, James H, Davis-Harrison, Rebecca L, Tavoosi, Narjes, Ke, Ke, Pureza, Vincent, Boettcher, John M, Clay, Mary C, Rienstra, Chad M, Ohkubo, Y. Zenmei, Pogorelov, Taras V, Tajkhorshid, Emad
Format Journal Article
LanguageEnglish
Published United States Elsevier Ltd 01.04.2010
Subjects
Algorithms
Blood Coagulation
Cell Membrane - metabolism
Computer Simulation
Factor VIIa
Factor VIIa - chemistry
Hematology, Oncology and Palliative Medicine
Humans
Magnetic Resonance Spectroscopy - methods
Membranes
Models, Biological
Nanotechnology - methods
NMR
Phospholipids
Phospholipids - chemistry
Protein Structure, Tertiary
Proteins - chemistry
Serine Proteases - chemistry
Thromboplastin - metabolism
Tissue Factor
Tissue Factor
Membranes
NMR
Phospholipids
Factor VIIa
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Summary:Abstract 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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:0049-3848
1879-2472
DOI:10.1016/j.thromres.2010.01.027