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2V3Q

Serendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein

Replaces:  2CAP
Summary for 2V3Q
Entry DOI10.2210/pdb2v3q/pdb
DescriptorHUMAN PHOSPHATE BINDING PROTEIN, GLYCEROL, PHOSPHATE ION, ... (5 entities in total)
Functional Keywordsatherosclerosis, hdl, missing gene, paraoxonase, phosphatemia, transport protein, transporter
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationSecreted : P85173
Total number of polymer chains1
Total formula weight39771.22
Authors
Primary citationDiemer, 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: 18076037
DOI: 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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