7I1B
HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1 BETA IN SOLUTION BY THREE-AND FOUR-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Summary for 7I1B
| Entry DOI | 10.2210/pdb7i1b/pdb |
| Descriptor | INTERLEUKIN-1 BETA (2 entities in total) |
| Functional Keywords | cytokine |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P01584 |
| Total number of polymer chains | 1 |
| Total formula weight | 17395.83 |
| Authors | Clore, G.M.,Gronenborn, A.M. (deposition date: 1991-01-22, release date: 1992-10-15, Last modification date: 2024-05-22) |
| Primary citation | Clore, G.M.,Wingfield, P.T.,Gronenborn, A.M. High-resolution three-dimensional structure of interleukin 1 beta in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy. Biochemistry, 30:2315-2323, 1991 Cited by PubMed Abstract: The determination of the high-resolution three-dimensional solution structure of interleukin 1 beta (IL-1 beta), a protein of 153 residues and 17.4 kDa, which plays a central role in the immune and inflammatory responses, has been determined by heteronuclear (13C and 15N) three- and four-dimensional NMR spectroscopy. The structure is based on 3146 experimental restraints comprising 2780 distance and 366 torsion angle (phi, psi, and chi 1) restraints. A total of 32 simulated annealing structures are calculated, and the atomic RMS distribution about the mean coordinate positions is 0.41 +/- 0.04 A for the backbone atoms and 0.82 +/- 0.04 A for all atoms (excluding residue 1 at the N-terminus and residues 152 and 153 at the C-terminus, which are partially disordered). In the case of internal side chains with a surface accessibility of less than or equal to 40%, the atomic RMS distribution about the mean coordinate positions for all atoms is 0.49 +/- 0.03 A. IL-1 beta resembles a tetrahedron and is composed of 12 beta-strands arranged in three pseudosymmetric topological units, each of which comprises 5 strands. Analysis of the mutational data on IL-1 beta in the light of the three-dimensional structure suggests the presence of three distinct binding sites for the IL-1 receptor on the surface of the protein. It is suggested that each of the three immunoglobulin domains which comprise the extracellular portion of the IL-1 receptor recognizes one of these sites. PubMed: 2001363DOI: 10.1021/bi00223a005 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
