2I1B

CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION

2I1B の概要

• エントリーDOI: 10.2210/pdb2i1b/pdb
• 分子名称: INTERLEUKIN-1 BETA (2 entities in total)
• 機能のキーワード: cytokine
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17395.83

構造登録者

Priestle, J.P.,Schaer, H.-P.,Gruetter, M.G. (登録日: 1990-01-02, 公開日: 1990-04-15, 最終更新日: 2024-02-21)

主引用文献

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

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: 2602367
DOI: 10.1073/pnas.86.24.9667

実験手法

X-RAY DIFFRACTION (2 Å)