Model structures and action of interleukin 1 and its antagonist.
A comparison has been made between the homology and hydrophobicity profiles of six interleukin amino acid sequences and that of the human interleukin 1 beta (IL-1 beta) for which a crystal structure exists. The resulting sequence alignment was used to build model structures for the sequences for three IL-1 alpha, two IL-1 beta and an interleukin receptor antagonist. Analysis of these structures demonstrates that the interleukin molecule has a strong electric dipole which is generated by the topological position of the amino acids in the sequence. Electrostatic surface calculations implicate a particular residues (Lys145) as being fundamental to interleukin activity and this supports site-directed mutation evidence that this residue is required for activity.
Oldfield
T J
TJ
Department of Chemistry, University of York, Heslington, UK.
Murray-Rust
P
P
Hubbard
R E
RE
D000595:Amino Acid Sequence; D053590:Interleukin 1 Receptor Antagonist Protein; D007375:Interleukin-1 / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017472:Receptors, Interleukin-1 / Q000037:antagonists & inhibitors*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012795:Sialoglycoproteins / Q000737:chemistry*
C507763:IL1RN protein, human; D053590:Interleukin 1 Receptor Antagonist Protein; D007375:Interleukin-1; D017472:Receptors, Interleukin-1; D012795:Sialoglycoproteins