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Factor XI Homodimer Structure Is Essential for Normal Proteolytic Activation by Factor XIIa, Thrombin, and Factor XIa
Coagulation factor XI (FXI) is a covalent homodimer consisting of two identical subunits of 80 kDa linked by a disulfide bond formed by Cys-321 within the Apple 4 domain of each subunit. Because FXI(C321S) is a noncovalent dimer, residues within the interface between the two subunits must mediate it...
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| Hoofdauteurs: | , , , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Biochemistry and Molecular Biology
2008
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2441546/ https://ncbi.nlm.nih.gov/pubmed/18441012 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M802275200 |
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