Title : Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains.

Pub. Date : 2001 Sep 14

PMID : 11454874






5 Functional Relationships(s)
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1 Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains. Disulfides CD47 molecule Homo sapiens
2 Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains. Disulfides CD47 molecule Homo sapiens
3 Conservation of Cys residues among CD47 homologues suggested the existence of a disulfide bond between the Ig and MMS domains that was confirmed by chemical digestion and mapped to Cys(33) and Cys(263). Disulfides CD47 molecule Homo sapiens
4 Mutagenesis to prevent formation of this disulfide completely disrupted CD47 signaling independent of effects on ligand binding, as assessed by T cell interleukin-2 secretion and Ca(2+) responses. Disulfides CD47 molecule Homo sapiens
5 Thus, a disulfide bond between the Ig and MMS domains of CD47 is required for normal ligand binding and signal transduction. Disulfides CD47 molecule Homo sapiens