Conformation of the propeptide domain of factor IX

Jya Wei Cheng, Chinpan Chen, Tai Huang Huang, Shan Ho Chou, Shi Han Chen

研究成果: 雜誌貢獻文章同行評審

4 引文 斯高帕斯(Scopus)

摘要

The propeptide domain in the precursor forms of blood clotting proteins contains the recognition sequences for γ-carboxylase. In hemophilia B, several point mutations in this propeptide domain are responsible for the inherited disease. A peptide containing the propeptide sequence of factor IX was synthesized by solid phase methods. Two dimensional 1H-NMR and CD studies indicate that this peptide motif adopts an α-helical structure in a 40% trifluoroethanol-containing aqueous solution. The results suggest that the amphipathic α-helix within the propeptide domain of factor IX could create a recognition surface for γ-carboxylase. The influences of mutations and their relationship with the α-helical structure are discussed.

原文英語
頁(從 - 到)227-231
頁數5
期刊BBA - General Subjects
1245
發行號2
DOIs
出版狀態已發佈 - 1995 十月 19

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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