2mib
From Proteopedia
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THE STRUCTURE OF MURINE INTERLEUKIN-1 BETA AT 2.8 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of recombinant murine interleukin-1 beta, has been solved by X-ray crystallographic techniques to 2.8 A resolution, and refined to a crystallographic R factor of 0.192. Although murine, interleukin-1 beta crystallizes in the same space group as human, interleukin-1 beta with almost identical unit cell dimensions, the packing, of the molecules is quite different. The murine interleukin-1 beta, structure was solved by molecular replacement using the refined structure, of human interleukin-1 beta as trial structure, and found to be related to, the human structure by a nearly perfect twofold rotation about the, crystallographic y-axis and a 14 degrees rotation about the z-axis, with, no translation. The folding of murine interleukin-1 beta is similar to, that found for the human variant, consisting of 12 beta strands wrapped, around a core of hydrophobic side chains in a tetrahedron-like fashion., Significant differences with respect to the human structure are seen at, the N terminus and in 4 of the 11 loops connecting the 12 beta strands.
About this Structure
2MIB is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The structure of murine interleukin-1 beta at 2.8 A resolution., van Oostrum J, Priestle JP, Grutter MG, Schmitz A, J Struct Biol. 1991 Oct;107(2):189-95. PMID:1807351
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