Model structures and action of interleukin 1 and its antagonist |
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Authors: | Oldfield, Thomas J. Murray-Rust, Peter Hubbard, Roderick E. |
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Affiliation: | 1Department of Chemistry, University of York Heslington, York YO1 5DD 2Glaxo Group Research Limited Greenford Road, Greenford, Middlesex UB6 OHE, UK |
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Abstract: | A comparison has been made between the homology and hydrophobkityprofiles of six interleukin amino add sequences and that ofthe human interleukin 1ß (IL-lß) for whicha crystal structure exists. The resulting sequence alignmentwas used to build model structures for the sequences for threeIL-l, two IL-1ß and an interleukin receptor antagonist.Analysis of these structures demonstrates that the interleukinmolecule has a strong electric dipole which is generated bythe topological position of the amino acids in the sequence.Electrostatic surface calculations implicate a particular residues(Lysl45) as being fundamental to interleukin activity and thissupports site-directed mutation evidence that this residue isrequired for activity. |
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Keywords: | interleukin/ electrostatics/ homology modelling/ hydrophobic profiles |
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