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| | <StructureSection load='4ot2' size='340' side='right'caption='[[4ot2]], [[Resolution|resolution]] 2.42Å' scene=''> | | <StructureSection load='4ot2' size='340' side='right'caption='[[4ot2]], [[Resolution|resolution]] 2.42Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ot2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OT2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OT2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ot2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OT2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NPS:(2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC+ACID'>NPS</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NPS:(2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC+ACID'>NPS</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f5u|4f5u]], [[4f5t|4f5t]], [[4j2v|4j2v]]</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=4ot2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ot2 OCA], [https://pdbe.org/4ot2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ot2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ot2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ot2 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=4ot2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ot2 OCA], [http://pdbe.org/4ot2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ot2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ot2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ot2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ALBU_HORSE ALBU_HORSE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Equus caballus]] | | [[Category: Equus caballus]] |
| | [[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: Fatty acid]]
| + | |
| - | [[Category: Helical]]
| + | |
| - | [[Category: Metabolites and drug]]
| + | |
| - | [[Category: Naproxen]]
| + | |
| - | [[Category: Plasma]]
| + | |
| - | [[Category: Serum albumin superfamily]]
| + | |
| - | [[Category: Three-domain protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
ALBU_HORSE
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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