2int
From Proteopedia
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[[Image:2int.gif|left|200px]] | [[Image:2int.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4''' | '''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4''' | ||
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[[Category: Walter, M R.]] | [[Category: Walter, M R.]] | ||
[[Category: Zhao, B G.]] | [[Category: Zhao, B G.]] | ||
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Revision as of 04:41, 4 May 2008
CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4
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.
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 Sun May 4 07:41:48 2008