2MIB
THE STRUCTURE OF MURINE INTERLEUKIN-1 BETA AT 2.8 ANGSTROMS RESOLUTION
Summary for 2MIB
| Entry DOI | 10.2210/pdb2mib/pdb |
| Related | 4ILB |
| Descriptor | INTERLEUKIN-1 BETA (2 entities in total) |
| Functional Keywords | cytokine |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm, cytosol : P10749 |
| Total number of polymer chains | 1 |
| Total formula weight | 17415.88 |
| Authors | Priestle, J.P.,Van Oostrum, J.,Schmitz, A.,Gruetter, M.G. (deposition date: 1993-12-06, release date: 1994-01-31, Last modification date: 2024-02-21) |
| Primary citation | van Oostrum, J.,Priestle, J.P.,Grutter, M.G.,Schmitz, A. The structure of murine interleukin-1 beta at 2.8 A resolution. J.Struct.Biol., 107:189-195, 1991 Cited by PubMed Abstract: The three-dimensional structure of recombinant murine interleukin-1 beta has been solved by X-ray crystallographic techniques to 2.8 A resolution and refined to a crystallographic R factor of 0.192. Although murine interleukin-1 beta crystallizes in the same space group as human interleukin-1 beta with almost identical unit cell dimensions, the packing of the molecules is quite different. The murine interleukin-1 beta structure was solved by molecular replacement using the refined structure of human interleukin-1 beta as trial structure, and found to be related to the human structure by a nearly perfect twofold rotation about the crystallographic y-axis and a 14 degrees rotation about the z-axis, with no translation. The folding of murine interleukin-1 beta is similar to that found for the human variant, consisting of 12 beta strands wrapped around a core of hydrophobic side chains in a tetrahedron-like fashion. Significant differences with respect to the human structure are seen at the N terminus and in 4 of the 11 loops connecting the 12 beta strands. PubMed: 1807351DOI: 10.1016/1047-8477(91)90021-N PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.84 Å) |
Structure validation
Download full validation report






