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Author(s) -
Dekker Frank J.,
de Mol Nico J.,
van Ameijde Jeroen,
Fischer Marcel J. E.,
Ruijtenbeek Rob,
Redegeld Frank A. M.,
Liskamp Rob M. J.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020301)3:2/3<115::aid-cbic115>3.0.co;2-j
Subject(s) - syk , sh2 domain , chemistry , mast cell , protein–protein interaction , tyrosine , biochemistry , signal transduction , receptor tyrosine kinase , biology , microbiology and biotechnology , tyrosine kinase , immunology
The cover picture shows an important protein–protein interaction in the mast cell which can lead to allergy, an excessive undesired immune response. In the mast cell the interaction between the diphosphorylated immunoreceptor tyrosine‐based activation motif of the immunoglobulin E—formed after exposure to an allergen—binding receptor and the Syk SH2 domain represents a crucial step in the signal transduction cascade eventually leading to the release of inflammatory mediators like histamine. Molecular constructs which are capable of strongly interfering with crucial protein–protein interactions might prevent the allergic response. The challenges in the preparation of these molecular constructs are introduction of the divalent interaction—required for a high affinity—and reduction of the peptidic character. In the shown molecular construct capable of interacting with the Syk SH2 domain, two weakly interacting monophosphorylated peptides are linked by a oligoethylene glycol spacer (shown in yellow). The length of the spacer was tuned by design and thus a heptapeptide sequence could be substituted. Further details can be found in the article by Liskamp and co‐workers on p. 238 ff.