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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
Author(s) -
Edwards Yvonne J.K.,
Perkins Stephen J.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01447-9
Subject(s) - helix (gastropod) , chemistry , von willebrand factor , fold (higher order function) , protein structure , protein secondary structure , beta sheet , crystallography , stereochemistry , biology , biochemistry , mechanical engineering , ecology , platelet , snail , engineering , immunology
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 Mg 2+ ‐binding Asp residues, two disulphide‐bridged Cys residues, and other known functional attributes of this domain.