G to S amino acid substitution in the β turn at residue 15 of the paired domain domain. This mutation has been shown to abolish DNA binding in vitro (FBrf0054064).
Comments on Models/Modifiers Based on Experimental Evidence
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Disease-implicated variant(s)
Phenotypic Data
Phenotypic Class
Phenotype Manifest In
Detailed Description
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Reference
Cannot provide prd function in an adult rescue assay. Shows no transcomplementation with prdNQ. Can antagonize endogenous prd function, causing a dominant, partially penetrant, prd phenocopy in embryos.
Carried in plasmid "Prd-GS", expressed in Schneider cells and tested for the proteins ability to transactivate through either the prd domain (PD) binding sites or the NP6 monomeric homeodomain binding sites by assaying Ecol\CAT activity levels.
Carried in plasmid "Prd-GS", expressed in Schneider cells and tested for the proteins ability to transactivate through either the prd domain (PD) binding sites or the NP6 monomeric homeodomain binding sites by assaying Ecol\CAT activity levels.