J. P. Priestle

Publication List Details

Period

1993 - 1997

Number

15

Co-Authors

A mutational analysis of receptor binding sites of interleukin-1{beta}:differences in binding of human interleukin-1{beta} muteins to human and mouse receptors (1994)

Grütter, M.G., Oostrum, J.van, Priestle, J.P., Edelmann, E., Joss, U., Feige, U., ...

The 3-D crystal structure of interleukin-1β(IL-1β) has been used to define its receptor binding surface by mutational analysis. The surface of IL-1β was probed by site-directed mutagenesis. A...

Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.

Priestle, J P, Schär, H P, Grütter, M G

The structure of human recombinant interleukin 1 beta (IL-1 beta) has been refined by a restrained least-squares method to a crystallographic R factor of 17.2% to 2.0 A resolution. One-hundred...

Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli.

Priestle, J P, Grütter, M G, White, J L, Vincent, M G, Kania, M, Wilson, E, ...

N-(5'-Phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli is a monomeric bifunctional enzyme of Mr 49,500 that catalyzes two sequential reactions in the...

Crystal structure of the cytokine interleukin-1 beta.

Priestle, J P, Schär, H P, Grütter, M G

The crystal structure of human recombinant interleukin-1 beta has been determined at 3.0 A resolution by the isomorphous replacement method in conjunction with solvent flattening techniques. The...

Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition.

Grütter, M G, Priestle, J P, Rahuel, J, Grossenbacher, H, Bode, W, Hofsteenge, J, ...

Thrombin is a serine protease that plays a central role in blood coagulation. It is inhibited by hirudin, a polypeptide of 65 amino acids, through the formation of a tight, noncovalent complex....

Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.

Priestle, J P, Schär, H P, Grütter, M G

The structure of human recombinant interleukin 1 beta (IL-1 beta) has been refined by a restrained least-squares method to a crystallographic R factor of 17.2% to 2.0 A resolution. One-hundred...

Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli.

Priestle, J P, Grütter, M G, White, J L, Vincent, M G, Kania, M, Wilson, E, ...

N-(5'-Phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli is a monomeric bifunctional enzyme of Mr 49,500 that catalyzes two sequential reactions in the...

Crystal structure of the cytokine interleukin-1 beta.

Priestle, J P, Schär, H P, Grütter, M G

The crystal structure of human recombinant interleukin-1 beta has been determined at 3.0 A resolution by the isomorphous replacement method in conjunction with solvent flattening techniques. The...

Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition.

Grütter, M G, Priestle, J P, Rahuel, J, Grossenbacher, H, Bode, W, Hofsteenge, J, ...

Thrombin is a serine protease that plays a central role in blood coagulation. It is inhibited by hirudin, a polypeptide of 65 amino acids, through the formation of a tight, noncovalent complex....

Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms.

Priestle, J. P., Rahuel, J., Rink, H., Tones, M., Grütter, M. G.

The three-dimensional structures of D-Phe-Pro-Arg-chloromethyl ketone-inhibited thrombin in complex with Tyr-63-sulfated hirudin (ternary complex) and of thrombin in complex with the bifunctional...

The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding.

Mittl, P. R., Priestle, J. P., Cox, D. A., McMaster, G., Cerletti, N., Grütter, M. G.

Transforming growth factors beta belong to a group of cytokines that control cellular proliferation and differentiation. Five isoforms are known that share approximately 75% sequence identity, but...

Recombinant hirustasin: production in yeast, crystallization, and interaction with serine proteases.

Di Marco, S., Fendrich, G., Knecht, R., Strauss, A., Pohlig, G., Heim, J., ...

A synthetic gene coding for the 55-amino acid protein hirustasin, a novel tissue kallikrein inhibitor from the leech Hirudo medicinalis, was generated by polymerase chain reaction using overlapping...