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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-844B-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-844C-5
Genre: Journal Article
Alternative Title : Prot Sci

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 Creators:
Manjasetty, Babu A., Author
Büssow, Konrad1, Author              
Fieber-Erdmann, Martin, Author
Roske, Yvette, Author
Gobom, Johan1, Author              
Scheich, Christoph2, Author
Götz, Frank, Author
Niesen, Frank H., Author
Heinemann, Udo, Author
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Max Planck Society, ou_persistent13              

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Free keywords: PTD012 family; alternative splicing; splice variant; structural genomics; Zn-binding site; ester hydrolase
 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.

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Language(s): deu - German
 Dates: 2006-04
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 305796
 Degree: -

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Title: Protein Science
  Alternative Title : Prot Sci
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 15 Sequence Number: - Start / End Page: 914 - 920 Identifier: -