Linked Life Data

8073036

Source:http://linkedlifedata.com/resource/pubmed/id/8073036

Statements in which the resource exists.
SubjectPredicateObjectContext
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pubmed-article:8073036pubmed:abstractTextThe 3-D crystal structure of interleukin-1 beta (IL-1 beta) has been used to define its receptor binding surface by mutational analysis. The surface of IL-1 beta was probed by site-directed mutagenesis. A total of 27 different IL-1 beta muteins were constructed, purified and analyzed. Receptor binding measurements on mouse and human cell lines were performed to identify receptor affinities. IL-1 beta muteins with modified receptor affinity were evaluated for structural integrity by CD spectroscopy or X-ray crystallography. Changes in six surface loops, as well as in the C- and N-termini, yielded muteins with lower binding affinities. Two muteins with intact binding affinities showed 10- to 100-fold reduced biological activity. The surface region involved in receptor binding constitutes a discontinuous area of approximately 1000 A2 formed by discontinuous polypeptide chain stretches. Based on these results, a subdivision into two distinct local areas is proposed. Differences in receptor binding affinities for human and mouse receptors have been observed for some muteins, but not for wild-type IL-1 beta. This is the first time a difference in binding affinity of IL-1 beta muteins to human and mouse receptors has been demonstrated.lld:pubmed
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pubmed-article:8073036pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:8073036pubmed:articleTitleA mutational analysis of receptor binding sites of interleukin-1 beta: differences in binding of human interleukin-1 beta muteins to human and mouse receptors.lld:pubmed
pubmed-article:8073036pubmed:affiliationDepartment of Biotechnology, Ciba-Geigy Ltd, Basle, Switzerland.lld:pubmed
pubmed-article:8073036pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8073036pubmed:publicationTypeComparative Studylld:pubmed
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