2V3Q
Serendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein
Replaces: 2CAPSummary for 2V3Q
Entry DOI | 10.2210/pdb2v3q/pdb |
Descriptor | HUMAN PHOSPHATE BINDING PROTEIN, GLYCEROL, PHOSPHATE ION, ... (5 entities in total) |
Functional Keywords | atherosclerosis, hdl, missing gene, paraoxonase, phosphatemia, transport protein, transporter |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Secreted : P85173 |
Total number of polymer chains | 1 |
Total formula weight | 39771.22 |
Authors | Morales, R.,Berna, A.,Carpentier, P.,Elias, M.,Contreras-Martel, C.,Renault, F.,Nicodeme, M.,Chesne-Seck, M.-L.,Bernier, F.,Dupuy, J.,Schaeffer, C.,Diemer, H.,Van Dorsselaer, A.,Fontecilla, J.C.,Masson, P.,Rochu, D.,Chabriere, E. (deposition date: 2007-06-20, release date: 2008-07-22, Last modification date: 2024-10-23) |
Primary citation | Diemer, H.,Elias, M.,Renault, F.,Rochu, D.,Contreras-Martel, C.,Schaeffer, C.,Van Dorsselaer, A.,Chabriere, E. Tandem Use of X-Ray Crystallography and Mass Spectrometry to Obtain Ab Initio the Complete and Exact Amino Acids Sequence of Hpbp, a Human 38kDa Apolipoprotein Proteins: Struct., Funct., Bioinf., 71:1708-, 2008 Cited by PubMed 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. PubMed: 18076037DOI: 10.1002/PROT.21866 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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