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==Crystal Structure of Equine Serum Albumin in complex with 3,5-diiodosalicylic acid== | ==Crystal Structure of Equine Serum Albumin in complex with 3,5-diiodosalicylic acid== | ||
<StructureSection load='4j2v' size='340' side='right' caption='[[4j2v]], [[Resolution|resolution]] 2.12Å' scene=''> | <StructureSection load='4j2v' size='340' side='right' caption='[[4j2v]], [[Resolution|resolution]] 2.12Å' scene=''> | ||
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</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=DIU:2-HYDROXY-3,5-DIIODO-BENZOIC+ACID'>DIU</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | </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=DIU:2-HYDROXY-3,5-DIIODO-BENZOIC+ACID'>DIU</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f5s|4f5s]], [[4f5t|4f5t]], [[4f5u|4f5u]], [[4jk4|4jk4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f5s|4f5s]], [[4f5t|4f5t]], [[4f5u|4f5u]], [[4jk4|4jk4]]</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=4j2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j2v RCSB], [http://www.ebi.ac.uk/pdbsum/4j2v PDBsum]</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=4j2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2v OCA], [http://pdbe.org/4j2v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j2v RCSB], [http://www.ebi.ac.uk/pdbsum/4j2v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j2v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4j2v" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 13:34, 11 August 2016
Crystal Structure of Equine Serum Albumin in complex with 3,5-diiodosalicylic acidCrystal Structure of Equine Serum Albumin in complex with 3,5-diiodosalicylic acid
Structural highlights
Publication Abstract from PubMedDue to their extraordinary binding properties, serum albumins are the main transporters of many small molecules in the circulatory system. Although all mammalian serum albumins exhibit quite high sequence similarity, their binding abilities are not the same. Until now, only human serum albumin (HSA) was subjected to extensive structural studies in complexes with various ligands. Here we present two crystal structures of the complexes of equine and bovine serum albumins with 3,5-diiodosalicylic acid (DIS), at resolutions 2.12A and 2.65A, respectively, and analyze interactions of the DIS ligand with both macromolecules. We highlight the differences in distribution of DIS binding sites between the bovine and equine serum albumins and compare results with the HSA binding ability of DIS and other structurally similar ligands. Crystallographic studies of the complexes of bovine and equine serum albumin with 3,5-diiodosalicylic acid.,Sekula B, Zielinski K, Bujacz A Int J Biol Macromol. 2013 Jun 12;60C:316-324. doi:, 10.1016/j.ijbiomac.2013.06.004. PMID:23769932[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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