IL1 structure

Crystallography by Priestle and colleagues indicated that IL-ip is a tetrahedron with the triangular faces formed by 12 p strands held together by hydrogen bonds. There are no intramolecular disulfide bonds. The hydrophobic core consists of side-chains arising from multiple positions along its primary sequence. The three-dimensional structure of IL-la is probably very similar to that of IL-ip, as they have a similar frictional ratio and Stokes radius. Both N- and C-termini are exposed and residues involved in receptor binding and activation are located in a number of sites over the surface of IL-1. At the amino acid sequence level, IL-lra is 26% homologous with II lp and 19% homologous with IL-la; the sequence of IL-ip is 26% identical to that of IL-la. The hyd-rophilicity plot of IL-lra is similar to that of IL-lp, indicating similarities in tertiary structure.

Deletion mutation studies by Mosley and coworkers suggested that the minimum polypeptide size for retaining biological activities for IL-la is 140 amino acids, extending from 128 through 267. The minimum size for IL-1 (3 is 147 amino acids, representing amino acids 120 through 266. Both minimal IL-1 forms require an arginine at the N-terminus to retain biological activity. Most attempts to identify smaller fragments of IL-1 have failed but a fragment of nine residues of human IL-ip (fragment 163-171) when fused to an antigen has been reported to have reproducible significant immunoadjuvant capacity. This fragment is absent from IL-lra.

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