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Crystal structure of recombinant human interleukin-4
M R Walter1, W J Cook, B G Zhao
1Department of Pathology, University of Alabama at Birmingham 35294.
The Journal of Biological Chemistry
|October 15, 1992
Summary
The crystal structure of recombinant human interleukin-4 (rhuIL-4) reveals a compact, globular protein featuring a four alpha-helix bundle. This detailed structural insight aids in understanding its biological function and receptor interactions.
Area of Science:
- Structural biology
- Protein crystallography
- Biochemistry
Background:
- Interleukin-4 (IL-4) is a critical cytokine involved in immune responses.
- Understanding the three-dimensional structure of rhuIL-4 is essential for elucidating its function.
Purpose of the Study:
- To determine the high-resolution crystal structure of recombinant human interleukin-4 (rhuIL-4).
- To characterize the structural features and propose regions involved in receptor binding.
Main Methods:
- X-ray crystallography
- Multiple isomorphous replacement
- Simulated annealing refinement
Main Results:
- The crystal structure of rhuIL-4 was refined to 2.35 A resolution.
- The structure exhibits a compact, globular fold dominated by a four alpha-helix bundle.
- A two-stranded antiparallel beta-sheet was identified within the connections of the alpha-helices.
- Structural similarities were noted with human granulocyte-macrophage colony-stimulating factor.
Conclusions:
- The determined structure provides a detailed atomic model of rhuIL-4.
- The structural characteristics suggest potential receptor binding sites.
- This structural information can guide future therapeutic development targeting IL-4 pathways.