Three-dimensional Structure of Tosyl-elastase

Amino-acid sequence studies and crystallographic evidence are used to construct an atomic model of elastase, which is compared with the structure of α-chymotrypsin. The single polypeptide chain of elastase is folded into two distinct and structurally similar halves displaying opposite polarity.

[1]  D. Blow,et al.  The study of alpha-chymotrypsin by x-ray diffraction. The Third CIBA Medal Lecture. , 1969, The Biochemical journal.

[2]  G. P. Hess,et al.  Implication of an ionizing group in the control of conformation and activity of chymotrypsin. , 1966, The Journal of biological chemistry.

[3]  B. Matthews,et al.  Structure of crystalline -chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanism. , 1968, Journal of molecular biology.

[4]  D M Shotton,et al.  The three-dimensional structure of crystalline porcine pancreatic elastase. , 1970, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[5]  H. Kaplan,et al.  Evidence that the activity of elastase is not dependent on the ionization of its N-terminal amino group. , 1969, Biochemical and biophysical research communications.

[6]  T. Steitz,et al.  The Structure of $\alpha$ -Chymotrypsin , 1970 .

[7]  B. Hartley Homologies in serine proteinases. , 1970, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[8]  B. Matthews,et al.  Three-dimensional Structure of Tosyl-α-chymotrypsin , 1967, Nature.

[9]  J. Kraut,et al.  Structure of Subtilisin BPN′ at 2.5 Å Resolution , 1969, Nature.

[10]  M. L. Bender,et al.  The elastase-catalyzed hydrolysis of p-nitrophenyl trimethylacetate. , 1968, Journal of the American Chemical Society.

[11]  D. Shotton,et al.  Amino-acid Sequence of Porcine Pancreatic Elastase and its Homologies with other Serine Proteinases , 1970, Nature.

[12]  D. Shotton,et al.  Three-dimensional Fourier Synthesis of Tosyl-elastase at 3.5 Å Resolution , 1970, Nature.

[13]  F M Richards,et al.  The matching of physical models to three-dimensional electron-density maps: a simple optical device. , 1968, Journal of molecular biology.

[14]  E. Shaw,et al.  Chromatography of trypsin and its derivatives. Characterization of a new active form of bovine trypsin. , 1968, The Journal of biological chemistry.

[15]  D. Blow,et al.  Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin , 1969, Nature.

[16]  G. Reeke,et al.  The structure of carboxypeptidase a, vi. Some results at 2.0-a resolution, and the complex with glycyl-tyrosine at 2.8-a resolution. , 1967, Proceedings of the National Academy of Sciences of the United States of America.

[17]  A. Narayanan,et al.  The specificity of purified porcine pancreatic elastase. , 1969, The Biochemical journal.

[18]  Thomas A. Steitz,et al.  Structure of crystalline α-chymotrypsin: III. Crystallographic studies of substrates and inhibitors bound to the active site of α-chymotrypsin , 1969 .

[19]  F. Sanger,et al.  Purification and specificity of pancreatic elastase. , 1961, The Biochemical journal.