Key residues at the membrane-distal surface of KACL, but not glycosylation, determine the functional interaction of the keratinocyte-specific C-type lectin-like receptor KACL with its high-affinity receptor NKp65.

Bauer, Björn; Spreu, Jessica; Rohe, Christina; Vogler, Isabel; Steinle, Alexander

Bauer, Björn; Spreu, Jessica; Rohe, Christina; Vogler, Isabel; Steinle, Alexander.

Affiliation

Bauer B; Institute for Molecular Medicine, Goethe-University Frankfurt am Main, Frankfurt am Main, Germany.

Immunology ; 145(1): 114-23, 2015 May.

Article in En | MEDLINE | ID: mdl-25510854

Subject(s)

Keratinocytes/immunology; Lectins, C-Type/immunology; Mutation, Missense; Receptors, NK Cell Lectin-Like/immunology; Amino Acid Substitution; Antibodies, Monoclonal, Murine-Derived/chemistry; Cells, Cultured; Glycosylation; Humans; Keratinocytes/cytology; Lectins, C-Type/genetics; Protein Binding/genetics; Protein Binding/immunology; Receptors, NK Cell Lectin-Like/genetics

Key words

epitope mapping; immune receptors; natural killer gene complex; skin

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Full text: 1 Database: MEDLINE Main subject: Keratinocytes / Mutation, Missense / Lectins, C-Type / Receptors, NK Cell Lectin-Like Limits: Humans Language: En Journal: Immunology Year: 2015 Type: Article Affiliation country: Germany

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