Predicted solution structure of zymogen human coagulation FVII

Journal of Computational Chemistry
L PereraL G Pedersen

Abstract

A model solution structure for the complete tissue factor-free calcium ion-bound human zymogen FVII (residues 1-406) (FVII) has been constructed to study possible conformational changes associated with the activation process and tissue factor (TF) binding. The initial structure for the present model was constructed using the X-ray crystallographic structure of human coagulation FVIIa/TF complex bound with calcium ions (Banner et al., Nature 1996, 380, 41-46). This model was subsequently subjected to lengthy molecular dynamics simulations. The Amber force field in conjunction with the PME electrostatic summation method was employed. The estimated TF free solution structure was then compared with the currently available X-ray crystal structures of FVIIa (with or without TF, variable inhibitor bound) to estimate the restructuring of FVII due to TF binding and activation. The solution structure of the zymogen FVII in the absence of TF is predicted to be an extended domain structure similar to that of the TF-bound X-ray crystal structure. An additional extension of the serine protease (SP) domain of the zymogen above a reference lipid surface by approximately 7 A was in agreement with experiment. Significant Gla-EGF1 and EGF1-EGF2 i...Continue Reading

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Citations

Jun 28, 2005·Journal of Thrombosis and Haemostasis : JTH·L Perera, L G Pedersen
Oct 28, 2015·PLoS Computational Biology·Lane W Votapka, Rommie E Amaro
Sep 28, 2006·Journal of Thrombosis and Haemostasis : JTH·C M ColinaL G Pedersen
May 12, 2012·Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis·Hye In WooHee-Jin Kim
Sep 13, 2007·Journal of Computational Chemistry·Karl N KirschnerRobert J Woods
Jul 8, 2020·Scientific Reports·Bosko M StojanovskiEnrico Di Cera

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