2ila: Difference between revisions
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[[Image:2ila.gif|left|200px]] | [[Image:2ila.gif|left|200px]] | ||
'''STRUCTURE OF INTERLEUKIN 1ALPHA AT 2.7-ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 2ila |SIZE=350|CAPTION= <scene name='initialview01'>2ila</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''STRUCTURE OF INTERLEUKIN 1ALPHA AT 2.7-ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2ILA is a [ | 2ILA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILA OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/2346741 2346741] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytokine]] | [[Category: cytokine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:30:48 2008'' | ||
Revision as of 15:30, 20 March 2008
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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
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