2I1B
CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION
Summary for 2I1B
| Entry DOI | 10.2210/pdb2i1b/pdb |
| Descriptor | INTERLEUKIN-1 BETA (2 entities in total) |
| Functional Keywords | cytokine |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 17395.83 |
| Authors | Priestle, J.P.,Schaer, H.-P.,Gruetter, M.G. (deposition date: 1990-01-02, release date: 1990-04-15, Last modification date: 2024-02-21) |
| Primary citation | Priestle, J.P.,Schar, H.P.,Grutter, M.G. Crystallographic refinement of interleukin 1 beta at 2.0 A resolution. Proc.Natl.Acad.Sci.USA, 86:9667-9671, 1989 Cited by PubMed Abstract: 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. PubMed: 2602367DOI: 10.1073/pnas.86.24.9667 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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