Three-dimensional crystal structure of recombinant murine interferon-beta
| Autor: | Yukio Mitsui, G. Kawano, S. Matsuda, K.T. Nakamura, T. Shimazu, Toshiya Senda, H. Shimizu |
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| Jazyk: | angličtina |
| Rok vydání: | 1992 |
| Předmět: |
Interleukin 2
Models Molecular Multiple isomorphous replacement Stereochemistry Protein Conformation Molecular Sequence Data Biology General Biochemistry Genetics and Molecular Biology law.invention Mice Protein structure law Sequence Homology Nucleic Acid medicine Animals Interferon gamma Amino Acid Sequence Binding site Molecular Biology Peptide sequence chemistry.chemical_classification Crystallography General Immunology and Microbiology General Neuroscience Interferon-beta Biological Evolution Recombinant Proteins Biochemistry chemistry Recombinant DNA Cytokines Glycoprotein medicine.drug Research Article |
| Popis: | The crystal structure of recombinant murine interferon-beta (IFN-beta) has been solved by the multiple isomorphous replacement method and refined to an R-factor of 20.5% against 2.6 A X-ray diffraction data. The structure shows a variant of the alpha-helix bundle with a new chain-folding topology, which seems to represent a basic structural framework of all the IFN-alpha and IFN-beta molecules belonging to the type I family. Functionally important segments of the polypeptide chain, as implied through numerous gene manipulation studies carried out so far, are spatially clustered indicating the binding site(s) to the receptor(s). Comparison of the present structure with those of other alpha-helical cytokine proteins, including porcine growth hormone, interleukin 2 and interferon gamma, indicated either a topological similarity in chain folding or a similar spatial arrangement of the alpha-helices. |
| Databáze: | OpenAIRE |
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