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Proposed structural models of the prothrombinase (FXa-FVa) complex

Autin, L ; Steen, Mårten LU ; Dahlbäck, Björn LU and Villoutreix, BO (2006) In Proteins 63(3). p.440-450
Abstract
Activated coagulation factor V (FVa) functions as a cofactor to factor Xa (FXa) in the conversion of prothrombin (PT) to thrombin. This essential procoagulant reaction, despite being the subject of extensive investigation, is not fully understood structurally and functionally. To elucidate the structure of the FXa-FVa complex, we have performed protein:protein (Pr:Pr) docking simulation with the pseudo-Brownian Pr:Pr docking ICM package and with the shape-complementarity Pr:Pr docking program PPD. The docking runs were carried out using a new model of full-length human FVa and the X-ray structure of human FXa. Five representative models of the FXa-FVa complex were in overall agreement with some of the available experimental data, but only... (More)
Activated coagulation factor V (FVa) functions as a cofactor to factor Xa (FXa) in the conversion of prothrombin (PT) to thrombin. This essential procoagulant reaction, despite being the subject of extensive investigation, is not fully understood structurally and functionally. To elucidate the structure of the FXa-FVa complex, we have performed protein:protein (Pr:Pr) docking simulation with the pseudo-Brownian Pr:Pr docking ICM package and with the shape-complementarity Pr:Pr docking program PPD. The docking runs were carried out using a new model of full-length human FVa and the X-ray structure of human FXa. Five representative models of the FXa-FVa complex were in overall agreement with some of the available experimental data, but only one model was found to be consistent with almost all of the reported experimental results. The use of hybrid docking approach (theoretical plus experimental) is definitively important to study such large macromolecular complexes. The FXa-FVa model we have created will be instrumental for further investigation of this macromolecular system and will guide future site directed mutagenesis experiments. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
activated Factor X, activated Factor V, structural docking, protein-protein interaction
in
Proteins
volume
63
issue
3
pages
440 - 450
publisher
John Wiley and Sons
external identifiers
  • wos:000236946200003
  • pmid:16437549
  • scopus:33646060435
  • pmid:16437549
ISSN
0887-3585
DOI
10.1002/prot.20848
language
English
LU publication?
yes
id
48676bbd-62e9-48df-b9d2-b7539525a88d (old id 411064)
date added to LUP
2016-04-01 15:55:55
date last changed
2021-09-05 03:33:34
@article{48676bbd-62e9-48df-b9d2-b7539525a88d,
  abstract     = {Activated coagulation factor V (FVa) functions as a cofactor to factor Xa (FXa) in the conversion of prothrombin (PT) to thrombin. This essential procoagulant reaction, despite being the subject of extensive investigation, is not fully understood structurally and functionally. To elucidate the structure of the FXa-FVa complex, we have performed protein:protein (Pr:Pr) docking simulation with the pseudo-Brownian Pr:Pr docking ICM package and with the shape-complementarity Pr:Pr docking program PPD. The docking runs were carried out using a new model of full-length human FVa and the X-ray structure of human FXa. Five representative models of the FXa-FVa complex were in overall agreement with some of the available experimental data, but only one model was found to be consistent with almost all of the reported experimental results. The use of hybrid docking approach (theoretical plus experimental) is definitively important to study such large macromolecular complexes. The FXa-FVa model we have created will be instrumental for further investigation of this macromolecular system and will guide future site directed mutagenesis experiments.},
  author       = {Autin, L and Steen, Mårten and Dahlbäck, Björn and Villoutreix, BO},
  issn         = {0887-3585},
  language     = {eng},
  number       = {3},
  pages        = {440--450},
  publisher    = {John Wiley and Sons},
  series       = {Proteins},
  title        = {Proposed structural models of the prothrombinase (FXa-FVa) complex},
  url          = {http://dx.doi.org/10.1002/prot.20848},
  doi          = {10.1002/prot.20848},
  volume       = {63},
  year         = {2006},
}