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Publication Detail
The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted β-sheet flanked by α-helices found in human ras-p21
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Edwards YJK, Perkins SJ
  • Publication date:
  • Pagination:
    283, 286
  • Journal:
    FEBS Letters
  • Volume:
  • Issue:
  • Status:
  • Print ISSN:
The von Willebrand Factor type A domain is the prototype for a protein superfamily. It possesses no significant sequence similarity to any known protein structure. Secondary structure predictions indicate a largely alternating pattern of six α-helices and six β-strands. A protein fold for this domain is proposed to correspond to a doubly-wound open twisted β-sheet structure flanked by α-helices. Close agreement was found with the GTP-binding domain of human ras-p21, provided that an extra α-helix was inserted. The structure of the predicted fold showed high compatibility with the proximate location of two Mg2+-binding Asp residues, two disulphide-bridged Cys residues, and other known functional attributes of this domain. © 1995.
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