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< | ==Serendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein== | ||
<StructureSection load='2v3q' size='340' side='right'caption='[[2v3q]], [[Resolution|resolution]] 1.89Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v3q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2cap 2cap]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V3Q FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3q OCA], [https://pdbe.org/2v3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v3q RCSB], [https://www.ebi.ac.uk/pdbsum/2v3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v3q ProSAT]</span></td></tr> | ||
</table> | |||
== Disease == | |||
[[https://www.uniprot.org/uniprot/PHBP_UNKP PHBP_UNKP]] May be involved in atherosclerosis. | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/PHBP_UNKP PHBP_UNKP]] Phosphate-binding protein.<ref>PMID:18076037</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v3/2v3q_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v3q ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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.,Diemer H, Elias M, Renault F, Rochu D, Contreras-Martel C, Schaeffer C, Van Dorsselaer A, Chabriere E Proteins. 2008 Jun;71(4):1708-20. PMID:18076037<ref>PMID:18076037</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2v3q" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphate-binding protein|Phosphate-binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Berna, A | [[Category: Large Structures]] | ||
[[Category: Bernier, F | [[Category: Berna, A]] | ||
[[Category: Carpentier, P | [[Category: Bernier, F]] | ||
[[Category: Chabriere, E | [[Category: Carpentier, P]] | ||
[[Category: Chesne-Seck, M L | [[Category: Chabriere, E]] | ||
[[Category: Contreras-Martel, C | [[Category: Chesne-Seck, M L]] | ||
[[Category: Diemer, H | [[Category: Contreras-Martel, C]] | ||
[[Category: Dorsselaer, A Van | [[Category: Diemer, H]] | ||
[[Category: Dupuy, J | [[Category: Dorsselaer, A Van]] | ||
[[Category: Elias, M | [[Category: Dupuy, J]] | ||
[[Category: Fontecilla, J C | [[Category: Elias, M]] | ||
[[Category: Masson, P | [[Category: Fontecilla, J C]] | ||
[[Category: Morales, R | [[Category: Masson, P]] | ||
[[Category: Nicodeme, M | [[Category: Morales, R]] | ||
[[Category: Renault, F | [[Category: Nicodeme, M]] | ||
[[Category: Rochu, D | [[Category: Renault, F]] | ||
[[Category: Schaeffer, C | [[Category: Rochu, D]] | ||
[[Category: Schaeffer, C]] | |||
[[Category: Atherosclerosis]] | [[Category: Atherosclerosis]] | ||
[[Category: Hdl]] | [[Category: Hdl]] | ||
| Line 49: | Line 63: | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
[[Category: Transporter]] | [[Category: Transporter]] | ||
Latest revision as of 15:37, 23 March 2022
Serendipitous discovery and X-ray structure of a human phosphate binding apolipoproteinSerendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein
Structural highlights
Disease[PHBP_UNKP] May be involved in atherosclerosis. Function[PHBP_UNKP] Phosphate-binding protein.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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.,Diemer H, Elias M, Renault F, Rochu D, Contreras-Martel C, Schaeffer C, Van Dorsselaer A, Chabriere E Proteins. 2008 Jun;71(4):1708-20. PMID:18076037[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Homo sapiens
- Large Structures
- Berna, A
- Bernier, F
- Carpentier, P
- Chabriere, E
- Chesne-Seck, M L
- Contreras-Martel, C
- Diemer, H
- Dorsselaer, A Van
- Dupuy, J
- Elias, M
- Fontecilla, J C
- Masson, P
- Morales, R
- Nicodeme, M
- Renault, F
- Rochu, D
- Schaeffer, C
- Atherosclerosis
- Hdl
- Missing gene
- Paraoxonase
- Phosphatemia
- Transport protein
- Transporter