Tandem use of X-ray crystallography and mass spectrometry to obtain ab initio the complete and exact amino acids sequence of HPBP, a human 38-kDa apolipoprotein

Hélène Diemer, Mikael Elias, Frédérique Renault, Daniel Rochu, Carlos Contreras-Martel, Christine Schaeffer, Alain Van Dorsselaer, Eric Chabriere

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

The Human Phosphate Binding Protein (HPBP) is a serendipitously discovered apolipoprotein from human plasma that binds phosphate. Amino acid sequence relates HPBP to an intriguing protein family that seems ubiquitous in eukaryotes. These proteins, named DING according to the sequence of their four conserved N-terminal residues, are systematically absent from eukaryotic genome databases. As a consequence, HPBP amino acids sequence had to be first assigned from the electronic density map. Then, an original approach combining X-ray crystallography and mass spectrometry provides the complete and a priori exact sequence of the 38-kDa HPBP. This first complete sequence of a eukaryotic DING protein will be helpful to study HPBP and the entire DING protein family.

Original languageEnglish (US)
Pages (from-to)1708-1720
Number of pages13
JournalProteins: Structure, Function and Genetics
Volume71
Issue number4
DOIs
StatePublished - Jun 2008

Keywords

  • Amino acids sequencing
  • Atherosclerosis
  • DING protein
  • Human phosphate binding protein
  • Mass spectrometry
  • Missing gene
  • X-ray crystallography

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