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2int
From Proteopedia
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(New page: 200px<br /> <applet load="2int" size="450" color="white" frame="true" align="right" spinBox="true" caption="2int, resolution 2.35Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 20:39, 12 November 2007
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CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4
Contents |
Overview
The crystal structure of recombinant human interleukin-4 (rhuIL-4) was, initially determined at 3.5-A resolution by multiple isomorphous, replacement techniques and subsequently refined to a resolution of 2.35 A, by simulated annealing. The final crystallographic R-factor, based on all, data in the range 6.0-2.35 A (7470 reflections), is 0.232. Bond lengths, and bond angles in the molecule have root mean square deviations from, ideal values of 0.016 A and 2.4 degrees, respectively. The overall, structure is highly compact and globular with a predominantly hydrophobic, core. The main structural feature of rhuIL-4 is a four alpha-helix bundle, which composes approximately 58% of the structure. The helices are, arranged in a left-handed antiparallel bundle with two overhand, connections. Within these connections is a two-stranded antiparallel, beta-sheet. Both the tertiary and secondary structures of rhuIL-4 are, similar to those of human granulocyte-macrophage colony-stimulating, factor. Critical regions for receptor binding are proposed.
Disease
Known diseases associated with this structure: AIDS, slow progression to OMIM:[147781], Atopy, susceptibility to OMIM:[147781]
About this Structure
2INT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of recombinant human interleukin-4., Walter MR, Cook WJ, Zhao BG, Cameron RP Jr, Ealick SE, Walter RL Jr, Reichert P, Nagabhushan TL, Trotta PP, Bugg CE, J Biol Chem. 1992 Oct 5;267(28):20371-6. PMID:1400355
Page seeded by OCA on Mon Nov 12 22:46:13 2007
