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Functional implications of interleukin‐1β based on the three‐dimensional structure
Author(s) -
Veerapandian B.,
Gilliland Gary L.,
Raag Reetta,
Svensson Anders L.,
Masui Yoshihiro,
Hirai Yoshikatsu,
Poulos Thomas L.
Publication year - 1992
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340120103
Subject(s) - antiparallel (mathematics) , barrel (horology) , chemistry , receptor , mutagenesis , molecule , biophysics , crystallography , stereochemistry , biology , biochemistry , materials science , physics , mutation , quantum mechanics , magnetic field , composite material , organic chemistry , gene
The molecular structure of interleukin‐1β, a hormone‐like cytokine with roles in several disease processes, has been determined at 2.0 Å resolution and refined to a crystallographic R ‐factor of 0.19. The frame‐work of this molecule consists of 12 antiparallel β‐strands exhibiting pseudo‐3‐fold symmetry. Six of the strands make up a β‐barrel with polar residues concentrated at either end. Analysis of the three‐dimensional structure, together with results from site‐directed mutagenesis and biochemical and immunological studies, suggest that the core of the β‐barrel plays an important functional role. A large patch of charged residues on one end of the barrel is proposed as the binding surface with which IL‐1 interacts with its receptor.