High-resolution three-dimensional structure of interleukin 1. beta. in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy
- National Inst. of Health, Bethesda, MD (United States)
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 ({sup 13}C and {sup 15}N) three- and four-dimensional NMR spectroscopy. The structure is based on 3,146 experimental restraints comprising 2,780 distance and 366 torsion angle ({phi}, {psi}, and {chi}{sub 1}) restraints. A total of 32 simulated annealing structures are calculated, and the atomic RMS distribution about the mean coordinate positions is 0.41 {plus minus} 0.04 {angstrom} for the backbone atoms and 0.82 {plus minus} 0.04 {angstrom} 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 {le} 40%, the atomic RMS distribution about the mean coordinate positions for all atoms is 0.49 {plus minus} 0.03 {angstrom}. 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.
- OSTI ID:
- 5623675
- Journal Information:
- Biochemistry; (United States), Vol. 30:9; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- English
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550201* - Biochemistry- Tracer Techniques