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Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.
Open accessAbstract
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 sixty-eight solvent molecules have been located, and isotropic temperature factors for each atom have been refined. The overall structure is composed of 12 beta-strands that can best be described as forming the four triangular faces of a tetrahedron with hydrogen bonding resembling normal antiparallel beta-sheets only at the vertices. The interior of this tetrahedron is filled by hydrophobic side chains. Analysis of sequence alignments with IL-1 beta from other mammalian species shows the interior to be very well conserved with the exterior residues markedly less so. There does not appear to be a clustering of invariant amino acid side chains on the surface of the molecule, suggesting an area of interaction with the IL-1 receptor. Comparison of the IL-1 beta structure with IL-1 alpha sequences indicates that IL-1 alpha probably has a similar overall folding as IL-1 beta but binds to the receptor in a different fashion. The three-dimensional structure of the IL-1 beta is analyzed in light of what has been suggested by previously published work on mutants and fragments of the molecule.
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Cited by
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Dinarello, C. (1991) · Blood · doi:10.1182/blood.v77.8.1627.1627 · Cited by 2,304
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Gabay, C., Lamacchia, C., & Palmer, G. (2010) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2010.4 · Cited by 897
IL-37 is a fundamental inhibitor of innate immunity
Nold, M. F., Nold-Petry, C. A., Zepp, J. A., Palmer, B. E., Bufler, P., & Dinarello, C. A. (2010) · Nature Immunology · doi:10.1038/ni.1944 · Cited by 849
Clore, G. M., Driscoll, P. C., Wingfield, P. T., & Gronenborn, A. M. (1990) · Biochemistry · doi:10.1021/bi00484a006 · Cited by 437
Evolutionary divergence and functions of the human interleukin (IL) gene family
Brocker, C., Thompson, D., Matsumoto, A., Nebert, D. W., & Vasiliou, V. (2010) · Human Genomics · doi:10.1186/1479-7364-5-1-30 · Cited by 368
Metadata
- Authors
- Priestle, J. P., Schär, H. P., & Grütter, M. G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1989-12
- Volume
- 86
- Issue
- 24
- Pages
- 9667-9671
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2011253952
- Cited by
- 165
- References
- 0
- FWCI
- 13.51
- Type
- journal article
- Language
- en
- Open access
- green
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- Priestle, J. P., Schär, H. P., & Grütter, M. G. (1989). Crystallographic refinement of interleukin 1 beta at 2.0 A resolution. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.24.9667
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