2i1b
CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION
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OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720]
About this StructureAbout this Structure
2I1B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic refinement of interleukin 1 beta at 2.0 A resolution., Priestle JP, Schar HP, Grutter MG, Proc Natl Acad Sci U S A. 1989 Dec;86(24):9667-71. PMID:2602367
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