Structural insights and ab initio sequencing within the DING proteins family

Mikael Elias, Dorothee Liebschner, Guillaume Gotthard, Eric Chabriere

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

DING proteins constitute an intriguing family of phosphate-binding proteins that was identified in a wide range of organisms, from prokaryotes and archae to eukaryotes. Despite their seemingly ubiquitous occurrence in eukaryotes, their encoding genes are missing from sequenced genomes. Such a lack has considerably hampered functional studies. In humans, these proteins have been related to several diseases, like atherosclerosis, kidney stones, inflammation processes and HIV inhibition. The human phosphate binding protein is a human representative of the DING family that was serendipitously discovered from human plasma. An original approach was developed to determine ab initio the complete and exact sequence of this 38 kDa protein by utilizing mass spectrometry and X-ray data in tandem. Taking advantage of this first complete eukaryotic DING sequence, a immunohistochemistry study was undertaken to check the presence of DING proteins in various mice tissues, revealing that these proteins are widely expressed. Finally, the structure of a bacterial representative from Pseudomonas fluorescens was solved at sub-angstrom resolution, allowing the molecular mechanism of the phosphate binding in these high-affinity proteins to be elucidated.

Original languageEnglish (US)
Pages (from-to)45-49
Number of pages5
JournalJournal of Synchrotron Radiation
Volume18
Issue number1
DOIs
StatePublished - Jan 2011
Externally publishedYes

Keywords

  • DING protein
  • HIV inhibition
  • ab initio sequencing
  • serendipity
  • sub-angstrom crystallography

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