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Probing inhibitor-i...
Probing inhibitor-induced conformational changes along the interface between tissue factor and factor VIIa
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- Osterlund, Maria (författare)
- Novo Nordisk AS, Prot Biotechnol, DK-2880 Bagsvaerd, Denmark Linkoping Univ, IFM, Dept Chem, Linkoping, Sweden Linkoping Univ, IFM, Dept Phys Chem, Linkoping, Sweden Novo Nordisk AS, Vasc Biochem, Malov, Denmark
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- Owenius, Rikard (författare)
- Linköpings universitet,Institutionen för fysik, kemi och biologi,Tekniska högskolan
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- Carlsson, Karin (författare)
- Linköpings universitet,Tekniska högskolan,Biokemi
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- Carlsson, Uno (författare)
- Linköpings universitet,Tekniska högskolan,Biokemi
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- Persson, Egon (författare)
- Vascular Biochemistry, Novo Nordisk A/S, Denmark
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- Lindgren, Mikael (författare)
- Department of Laser Systems, Division of Sensor Technology, Swedish Defence Research Agency, P.O. Box 1165, SE- 581 11 Linko¨ping, Sweden.
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- Freskgård, Per-Ola (författare)
- Linköpings universitet,Tekniska högskolan,Institutionen för fysik, kemi och biologi
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- Svensson, Magdalena (författare)
- Linköpings universitet,Tekniska högskolan,Biokemi
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(creator_code:org_t)
- 2001-07-12
- 2001
- Engelska.
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 40:31, s. 9324-9328
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Upon injury of a blood vessel, activated factor VII (FVIIa) forms a high-affinity complex with its allosteric regulator, tissue factor (TF), and initiates blood clotting. Active site-inhibited factor VIIa (FVIIai) binds to TF with even higher affinity. We compared the interactions of FVIIai and FVIIa with soluble TF (sTF). Six residues in sTF were individually selected for mutagenesis and site-directed labeling. The residues are distributed along the extensive binding interface, and were chosen because they are known to interact with the different domains of FVIIa. Fluorescent and spin probes were attached to engineered Cys residues to monitor local changes in hydrophobicity, accessibility, and rigidity in the sTF-FVIIa complex upon occupation of the active site of FVIIa. The results show that inhibition of FVIIa caused the structures around the positions in sTF that interact with the protease domain of FVIIa to become more rigid and less accessible to solvent. Thus, the presence of an active site inhibitor renders the interface in this region less flexible and more compact, whereas the interface between sTF and the light chain of FVIIa is unaffected by active site occupancy.
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- TECHNOLOGY
- TEKNIKVETENSKAP
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