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Sequence and structural relationships in the cytokine family
P Manavalan1, D L Swope, R M Withy
1Genzyme Corporation, Framingham, Massachusetts 01901.
Journal of Protein Chemistry
|June 1, 1992
Summary
Cytokine sequence alignment reveals conserved exon patterns and homologous regions, particularly in exon 4. Secondary structure predictions suggest a common four alpha-helical bundle structure in cytokines.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Cytokines, growth hormone, and prolactin are crucial signaling molecules.
- Understanding their structural and sequence similarities can elucidate conserved functions.
Purpose of the Study:
- To align and predict the secondary structure of nine cytokines, growth hormone, and prolactin.
- To identify conserved sequence patterns and homologous regions within these proteins.
Main Methods:
- Sequence alignment of nine cytokines, growth hormone, and prolactin.
- Secondary structure prediction using computational methods.
- Analysis of conserved residues and homologous regions.
Main Results:
- Identified characteristic sequence patterns in each exon shared by all cytokines.
- Observed significant sequence similarity in exon 4, with conserved Phe-Leu residue pair.
- Detected high homology between granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleukin 3 (IL-3).
- Predicted an antiparallel helix-turn-helix motif in exon 3 of all cytokines, forming a four alpha-helical bundle.
- Predicted topological connectivity for several cytokines based on structure and disulfide bonding.
Conclusions:
- Cytokines share conserved sequence patterns and structural motifs, suggesting a common evolutionary origin and functional mechanism.
- The predicted four alpha-helical bundle structure is a conserved feature among cytokines.
- Further structural and functional studies can be guided by these sequence and topological predictions.