The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted beta-sheet flanked by alpha-helices found in human ras-p21

FEBS Lett. 1995 Jan 30;358(3):283-6. doi: 10.1016/0014-5793(94)01447-9.


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 alpha-helices and six beta-strands. A protein fold for this domain is proposed to correspond to a doubly-wound open twisted beta-sheet structure flanked by alpha-helices. Close agreement was found with the GTP-binding domain of human ras-p21, provided that an extra alpha-helix was inserted. The structure of the predicted fold showed high compatibility with the proximate location of two Mg(2+)-binding Asp residues, two disulphide-bridged Cys residues, and other known functional attributes of this domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Humans
  • Molecular Sequence Data
  • Oncogene Protein p21(ras) / chemistry*
  • Protein Folding*
  • Protein Structure, Secondary*
  • Sequence Homology, Amino Acid
  • von Willebrand Factor / chemistry*


  • von Willebrand Factor
  • Oncogene Protein p21(ras)