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Journal Article

RNAi-mediated suppression of OCT4 function in human ES cell as a model for differentiation in the Blastocyst

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons50117

Büssow,  Konrad
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50168

Gobom,  Johan
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

Scheich,  Christoph
Max Planck Society;

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Citation

Manjasetty, B. A., Büssow, K., Fieber-Erdmann, M., Roske, Y., Gobom, J., Scheich, C., et al. (2006). RNAi-mediated suppression of OCT4 function in human ES cell as a model for differentiation in the Blastocyst. Protein Science, 15, 914-920.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-844B-7
Abstract
The human protein PTD012 is the longer product of an alternatively spliced gene and was described to be localized in the nucleus. The X-ray structure analysis at 1.7 Å resolution of PTD012 through SAD phasing reveals a monomeric protein and a novel fold. The shorter splice form was also studied and appears to be unfolded and non-functional. The structure of PTD012 displays an {alpha}betabeta{alpha} four-layer topology. A metal ion residing between the central beta-sheets is partially coordinated by three histidine residues. X-ray absorption near-edge structure (XANES) analysis identifies the PTD012-bound ion as Zn2+. Tetrahedral coordination of the ion is completed by the carboxylate oxygen atom of an acetate molecule taken up from the crystallization buffer. The binding of Zn2+ to PTD012 is reminiscent of zinc-containing enzymes such as carboxypeptidase, carbonic anhydrase, and beta-lactamase. Biochemical assays failed to demonstrate any of these enzyme activities in PTD012. However, PTD012 exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate.