Identification of the human yvh1 protein-tyrosine phosphatase orthologue reveals a novel zinc binding domain essential for in vivo function*

HIGHLIGHTS

• who: Marco Muda from the sites of pGEX, hYVH DC was obtained by PCR using a specific primer that introduces a stop codon at amino acid, . To generate an enzymatically inactive h, and hYVH CSDC the catalytic essential Cys, was mutated to a serine residue. Site-directed mutagenesis was performed using the Quick-Change Kit (Stratagene) according to manufacturer's instructions. The hYVH1, hYVH CS, hYVH DC, hYVH CSDC inserts were isolated from pGEX , using BamHI and XmaI and subcloned into p ADH (11). The XbaI fragment encoding YVH1, from pGE-KG/, was used to generate p . . .
  

   

  

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