Importance of individual residues in hydrophobic patch PLVIVGL (1481-1487) in FV-Short for synergistic TFPIα cofactor activity with protein S, an alanine-scanning study: AlphaFold-mediated prediction of FV-Short/TFPIα/protein S trimolecular complex s

Individual residues (V1483, I1484, G1486, and L1487) in the hydrophobic patch are demonstrated to be important for the synergistic TFPIα-cofactor activity and for the assembly of a trimolecular FXa-inhibitory complex.

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Journal
Journal of Thrombosis and Haemostasis
Published
2024-11-29
DOI
https://doi.org/10.1016/j.jtha.2024.11.013
Primary Topic
Blood Coagulation and Thrombosis Mechanisms
Type
article
Field-Weighted Citation Impact
0.00

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article

Importance of individual residues in hydrophobic patch PLVIVGL (1481-1487) in FV-Short for synergistic TFPIα cofactor activity with protein S, an alanine-scanning study: AlphaFold-mediated prediction of FV-Short/TFPIα/protein S trimolecular complex s

Björn Dahlbäck, Sinh Tran, Piotr Drączkowski
Journal of Thrombosis and Haemostasis
Blood Coagulation and Thrombosis Mechanisms
article

Importance of individual residues in hydrophobic patch PLVIVGL (1481-1487) in FV-Short for synergistic TFPIα cofactor activity with protein S, an alanine-scanning study: AlphaFold-mediated prediction of FV-Short/TFPIα/protein S trimolecular complex s

Björn Dahlbäck, Sinh Tran, Piotr Drączkowski
article en

Abstract

Individual residues (V1483, I1484, G1486, and L1487) in the hydrophobic patch are demonstrated to be important for the synergistic TFPIα-cofactor activity and for the assembly of a trimolecular FXa-inhibitory complex.

Journal of Thrombosis and HaemostasisVol. 23(3)
Stockholm University (SE), Malmö University (SE), Lund University (SE), Science for Life Laboratory (SE), Skåne University Hospital (SE)
Hjärt-Lungfonden, Knut och Alice Wallenbergs Stiftelse, Vetenskapsrådet, Science for Life Laboratory
Openalex Percentile: Top 65%
Blood Coagulation and Thrombosis Mechanisms
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