Structure of an interleukin-1.beta. mutant with reduced bioactivity shows multiple subtle changes in conformation that affect protein-protein recognition-Reference-Cited by-同舟云学术

Structure of an interleukin-1.beta. mutant with reduced bioactivity shows multiple subtle changes in conformation that affect protein-protein recognition

Published:1993-08-31 Issue:34 Volume:32 Page:8749-8757
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Camacho Nancy P.,Smith Deborah R.,Goldman Adrian,Schneider Bohdan,Green David,Young Peter R.,Berman Helen M.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00085a005

Reference47 articles.

1. Interleukin 1 receptor antagonist. A new member of the interleukin 1 family.

2. Multiple amino acid substitutions suggest a structural basis for the separation of biological activity and receptor binding in a mutant human interleukin-1.beta. protein

3. Mode of action of soybean trypsin inhibitor (Kunitz) as a model for specific protein–protein interactions

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