2ila
From Proteopedia
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STRUCTURE OF INTERLEUKIN 1ALPHA AT 2.7-ANGSTROMS RESOLUTION
Overview
The interleukin 1 (IL-1) family of proteins has a central role in, modulating immune and inflammatory responses. Two major IL-1 proteins, designated alpha (IL-1 alpha) and beta (IL-1 beta), are produced by, activated macrophages and other cell types. In an effort to understand the, similarities and differences in the physicochemical and functional, properties of these two proteins, a program was initiated to determine, their structures. Crystals of IL-1 alpha were grown, and the, three-dimensional structure at 2.7-A resolution was solved. The technique, of multiple-wavelength anomalous dispersion (MAD) with the, selenomethionine form of IL-1 alpha was utilized in combination with a, single mercury derivative to provide the starting phases. Partial, refinement of the IL-1 alpha model has been performed as well. The overall, structure is composed of 14 beta-strands and a 3(10) helix. The core of, this structure is a capped beta-barrell that possesses 3-fold symmetry and, displays a topology similar to that observed for IL-1 beta [Priestle, J., P., et al. (1988) EMBO J. 7, 339-343] and soybean trypsin inhibitor (STI), [McLachlan, A. D. (1979) J. Mol. Biol. 133, 557-563]. In this paper, the, overall structure of IL-1 alpha and the nature and fidelity of the, internal 3-fold symmetry are discussed. Comparisons with IL-1 beta and STI, are made within these contexts.
About this Structure
2ILA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of interleukin 1 alpha at 2.7-A resolution., Graves BJ, Hatada MH, Hendrickson WA, Miller JK, Madison VS, Satow Y, Biochemistry. 1990 Mar 20;29(11):2679-84. PMID:2346741
Page seeded by OCA on Mon Nov 12 22:45:38 2007
