4j2v: Difference between revisions
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== | ==Crystal Structure of Equine Serum Albumin in complex with 3,5-diiodosalicylic acid== | ||
[[4j2v]] is a 1 chain structure with sequence from [ | <StructureSection load='4j2v' size='340' side='right'caption='[[4j2v]], [[Resolution|resolution]] 2.12Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4j2v]] 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=4J2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J2V FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12Å</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=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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4j2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2v OCA], [https://pdbe.org/4j2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j2v RCSB], [https://www.ebi.ac.uk/pdbsum/4j2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j2v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ALBU_HORSE ALBU_HORSE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Due 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<ref>PMID:23769932</ref> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4j2v" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Albumin 3D structures|Albumin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Bujacz | [[Category: Large Structures]] | ||
[[Category: Bujacz | [[Category: Bujacz A]] | ||
[[Category: Sekula | [[Category: Bujacz G]] | ||
[[Category: Zielinski | [[Category: Sekula B]] | ||
[[Category: Zielinski K]] | |||
Latest revision as of 18:35, 20 September 2023
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
FunctionPublication 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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