کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5370914 | 1503918 | 2015 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A model for the unique role of factor Va A2 domain extension in the human ternary thrombin-generating complex A model for the unique role of factor Va A2 domain extension in the human ternary thrombin-generating complex](/preview/png/5370914.png)
- A complete human thrombin-generating model is developed.
- The factor Va A2 C-terminus with sulfotyrosines is crucial.
- The ternary model is solvent-equilibrated with molecular dynamics.
An all-atom human ternary model for the prothrombinase-prothrombin complex, including metal ions and post-translationally modified residues, was constructed from existing X-ray crystal structures. The factor Xa-prothrombin interface was taken from an existing ternary model, which locates the active site of factor Xa in the vicinity of prothrombin cleavage positions. The three sulfotyrosine residues at the C-terminal sequence of factor Va A2 domain are accommodated by modelling rational interactions with positively charged patches on the surface of prothrombin. The entire model is then solvent-equilibrated with molecular dynamics. This ternary model for the thrombin-generating complex provides an estimate as to the role of the C-terminus of the factor Va A2 domain: to establish an interface between FXa and prothrombin and to stabilize the orientation of this interface.
Journal: Biophysical Chemistry - Volume 199, April 2015, Pages 46-50