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Model structures and action of interleukin 1 and its antagonist
T J Oldfield1, P Murray-Rust, R E Hubbard
1Department of Chemistry, University of York, Heslington, UK.
Protein Engineering
|November 1, 1993
Summary
This study compares interleukin sequences, revealing a strong electric dipole in interleukin molecules. Lysine 145 is identified as crucial for interleukin activity, supported by mutation data.
Area of Science:
- Biochemistry
- Structural Biology
- Immunology
Background:
- Interleukin 1 beta (IL-1 beta) has a known crystal structure.
- Homology and hydrophobicity profiles of six other interleukin sequences were compared to IL-1 beta.
Purpose of the Study:
- To build model structures for various interleukin sequences.
- To analyze the structural and electrostatic properties of interleukin molecules.
- To identify key residues responsible for interleukin activity.
Main Methods:
- Sequence alignment of six interleukin sequences with human IL-1 beta.
- Building model structures for three IL-1 alpha, two IL-1 beta, and one interleukin receptor antagonist.
- Analysis of molecular structures, including electrostatic surface calculations.
Main Results:
- The study revealed a strong electric dipole within the interleukin molecule, attributed to amino acid positioning.
- Electrostatic surface analysis identified Lysine 145 (Lys145) as a critical residue for interleukin activity.
- These findings align with existing site-directed mutation data confirming Lys145's essential role.
Conclusions:
- The topological arrangement of amino acids in interleukin sequences generates a significant electric dipole.
- Lysine 145 is fundamentally important for the biological activity of interleukins.
- Structural and electrostatic analyses provide insights into interleukin function and guide further research.