In vitro maturation of Drosophila melanogaster Spätzle protein with refolded Easter reveals a novel cleavage site within the prodomain

Dorsoventral patterning during embryogenesis is mediated by a well-defined gradient of the mature NGF-like ligand Spätzle. Easter, the ultimate protease of a ventrally-restricted serine protease cascade, plays a key role in the regulation of the morphogenic gradient, catalyzing the activation cleava...

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Veröffentlicht in:	Biological chemistry 2013-08, Vol.394 (8), p.1069-1075
Hauptverfasser:	Ursel, Christian, Fandrich, Uwe, Hoffmann, Anita, Sieg, Torsten, Ihling, Christian, Stubbs, Milton T.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals cystine knot protein development Drosophila melanogaster - chemistry Drosophila melanogaster - metabolism Drosophila Proteins - chemistry Drosophila Proteins - metabolism embryonic morphogenesis Molecular Sequence Data prohormone activation protease specificity Protein Isoforms - chemistry Protein Isoforms - metabolism Protein Refolding Protein Structure, Tertiary Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism Toll signaling
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