Functional implications of interleukin-1 beta based on the three-dimensional structure. |
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Authors: | B Veerapandian G L Gilliland R Raag A L Svensson Y Masui Y Hirai T L Poulos |
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Institution: | Center for Advanced Research in Biotechnology, University of Maryland, Rockville. |
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Abstract: | The molecular structure of interleukin-1 beta, a hormone-like cytokine with roles in several disease processes, has been determined at 2.0 A resolution and refined to a crystallographic R-factor of 0.19. The framework of this molecule consists of 12 antiparallel beta-strands exhibiting pseudo-3-fold symmetry. Six of the strands make up a beta-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 beta-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. |
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Keywords: | crystallography molecular isomorphous replacement molecular dynamics refinement interleukin site-directed mutagenesis receptor-binding surface epitope |
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