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| | <StructureSection load='4or0' size='340' side='right'caption='[[4or0]], [[Resolution|resolution]] 2.58Å' scene=''> | | <StructureSection load='4or0' size='340' side='right'caption='[[4or0]], [[Resolution|resolution]] 2.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4or0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OR0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4or0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OR0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NPS:(2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC+ACID'>NPS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NPS:(2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC+ACID'>NPS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f5s|4f5s]], [[4jk4|4jk4]]</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=4or0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4or0 OCA], [https://pdbe.org/4or0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4or0 RCSB], [https://www.ebi.ac.uk/pdbsum/4or0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4or0 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4or0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4or0 OCA], [http://pdbe.org/4or0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4or0 RCSB], [http://www.ebi.ac.uk/pdbsum/4or0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4or0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALBU_BOVIN ALBU_BOVIN]] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. | + | [https://www.uniprot.org/uniprot/ALBU_BOVIN ALBU_BOVIN] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bujacz, A]] | + | [[Category: Bujacz A]] |
| - | [[Category: Bujacz, G]] | + | [[Category: Bujacz G]] |
| - | [[Category: Sekula, B]] | + | [[Category: Sekula B]] |
| - | [[Category: Zielinski, K]] | + | [[Category: Zielinski K]] |
| - | [[Category: Bovine serum albumin]]
| + | |
| - | [[Category: Bsa]]
| + | |
| - | [[Category: Drug]]
| + | |
| - | [[Category: Fatty acid]]
| + | |
| - | [[Category: Helical protein possessing three domain]]
| + | |
| - | [[Category: Hormone]]
| + | |
| - | [[Category: Metabolite]]
| + | |
| - | [[Category: Naproxen]]
| + | |
| - | [[Category: Plasma]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
ALBU_BOVIN Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.
Publication Abstract from PubMed
Serum albumin, a protein naturally abundant in blood plasma, shows remarkable ligand binding properties of numerous endogenous and exogenous compounds. Most of serum albumin binding sites are able to interact with more than one class of ligands. Determining the protein-ligand interactions among mammalian serum albumins is essential for understanding the complexity of this transporter. We present three crystal structures of serum albumins in complexes with naproxen (NPS): bovine (BSA-NPS), equine (ESA-NPS), and leporine (LSA-NPS) determined to 2.58 A (C2), 2.42 A (P61 ), and 2.73 A (P21 21 21 ) resolutions, respectively. A comparison of the structurally investigated complexes with the analogous complex of human serum albumin (HSA-NPS) revealed surprising differences in the number and distribution of naproxen binding sites. Bovine and leporine serum albumins possess three NPS binding sites, but ESA has only two. All three complexes of albumins studied here have two common naproxen locations, but BSA and LSA differ in the third NPS binding site. None of these binding sites coincides with the naproxen location in the HSA-NPS complex, which was obtained in the presence of other ligands besides naproxen. Even small differences in sequences of serum albumins from various species, especially in the area of the binding pockets, influence the affinity and the binding mode of naproxen to this transport protein.Proteins 2014. (c) 2014 Wiley Periodicals, Inc.
Structural studies of bovine, equine, and leporine serum albumin complexes with naproxen.,Bujacz A, Zielinski K, Sekula B Proteins. 2014 Apr 17. doi: 10.1002/prot.24583. PMID:24753230[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bujacz A, Zielinski K, Sekula B. Structural studies of bovine, equine, and leporine serum albumin complexes with naproxen. Proteins. 2014 Apr 17. doi: 10.1002/prot.24583. PMID:24753230 doi:http://dx.doi.org/10.1002/prot.24583
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