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

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.

[1]  C. Branden,et al.  Introduction to protein structure , 1991 .

[2]  S V Evans,et al.  SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. , 1993, Journal of molecular graphics.

[3]  B. Rost,et al.  Prediction of protein secondary structure at better than 70% accuracy. , 1993, Journal of molecular biology.

[4]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[5]  M. Arnaout,et al.  A novel divalent cation-binding site in the a domain of the β 2 integrin CR3 (CD11b/CD18) is essential for ligand binding , 1993, Cell.

[6]  A Valencia,et al.  The ras protein family: evolutionary tree and role of conserved amino acids. , 1991, Biochemistry.

[7]  P. Bonaldo,et al.  The superfamily of proteins with von Willebrand factor type A-like domains: one theme common to components of extracellular matrix, hemostasis, cellular adhesion, and defense mechanisms. , 1991, Blood.

[8]  D. T. Jones,et al.  A new approach to protein fold recognition , 1992, Nature.

[9]  J. Sadler.  von Willebrand factor. , 1991, The Journal of biological chemistry.

[10]  J. Garnier,et al.  Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. , 1978, Journal of molecular biology.

[11]  John P. Overington,et al.  Alignment and searching for common protein folds using a data bank of structural templates. , 1993, Journal of molecular biology.

[12]  T. Mattioli,et al.  Primary donor structure and interactions in bacterial reaction centers from near-infrared Fourier transform resonance Raman spectroscopy. , 1991, Biochemistry.

[13]  P. Y. Chou,et al.  Prediction of the secondary structure of proteins from their amino acid sequence. , 2006 .

[14]  T. P. Flores,et al.  Identification and classification of protein fold families. , 1993, Protein engineering.

[15]  C. Ward,et al.  Identification of aspartic acid 514 through glutamic acid 542 as a glycoprotein Ib-IX complex receptor recognition sequence in von Willebrand factor. Mechanism of modulation of von Willebrand factor by ristocetin and botrocetin. , 1992, Biochemistry.

[16]  Robert B Sim,et al.  A study of the structure of human complement component factor H by Fourier transform infrared spectroscopy and secondary structure averaging methods. , 1988, Biochemistry.

[17]  J. Richardson,et al.  The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.

[18]  W. Kabsch,et al.  Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation , 1989, Nature.

[19]  T L Blundell,et al.  Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. II. Secondary structures. , 1994, Journal of molecular biology.

[20]  W. Taylor,et al.  Identification of protein sequence homology by consensus template alignment. , 1986, Journal of molecular biology.

[21]  K. Titani,et al.  Identification of disulfide-bridged substructures within human von Willebrand factor. , 1987, Biochemistry.

[22]  R. Houghten,et al.  Structure of the von Willebrand factor domain interacting with glycoprotein Ib. , 1988, The Journal of biological chemistry.