2ydf: Difference between revisions

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-[[Image:2ydf.jpg|left|200px]]
-<!--
+==HUMAN SERUM ALBUMIN COMPLEXED WITH IOPHENOXIC ACID==
-The line below this paragraph, containing "STRUCTURE_2ydf", creates the "Structure Box" on the page.
+<StructureSection load='2ydf' size='340' side='right'caption='[[2ydf]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ydf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YDF FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IO3:IOPHENOXIC+ACID'>IO3</scene></td></tr>
-{{STRUCTURE_2ydf|  PDB=2ydf  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ydf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydf OCA], [https://pdbe.org/2ydf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydf RCSB], [https://www.ebi.ac.uk/pdbsum/2ydf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydf ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:[https://omim.org/entry/103600 103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.<ref>PMID:8048949</ref> <ref>PMID:7852505</ref> <ref>PMID:9329347</ref> <ref>PMID:9589637</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] 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.<ref>PMID:19021548</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+ABSTRACT: BACKGROUND: Iophenoxic acid is an iodinated radiocontrast agent that was withdrawn from clinical use because of its exceptionally long half-life in the body, which was due in part to its high-affinity binding to human serum albumin (HSA). It was replaced by Iopanoic acid, which has an amino rather than a hydroxyl group at position 3 on the iodinated benzyl ring and, as a result, binds to albumin with lower affinity and is excreted more rapidly from the body. To understand how iophenoxic acid binds so tightly to albumin, we wanted to examine the structural basis of its interaction with HSA. RESULTS: We have determined the co-crystal structure of HSA in complex with iophenoxic acid at 2.75 A resolution, revealing a total of four binding sites, two of which -- in drugs sites 1 and 2 on the protein -- are likely to be occupied at clinical doses. High-affinity binding of iophenoxic acid occurs at drug site 1. The structure reveals that polar and apolar groups on the compound are involved in its interactions with drug site 1. In particular, the 3-hydroxyl group makes three hydrogen bonds with the side-chains of Tyr 150 and Arg 257. The mode of binding to drug site 2 is similar except for the absence of a binding partner for the hydroxyl group on the benzyl ring of the compound. CONCLUSIONS: The HSA-iophenoxic acid structure indicates that high-affinity binding to drug site 1 is likely to be due to extensive desolvation of the compound, coupled with the ability of the binding pocket to provide a full set of salt-bridging or hydrogen bonding partners for its polar groups. Consistent with this interpretation, the structure also suggests that the lower-affinity binding of iopanoic acid arises because replacement of the 3-hydroxyl by an amino group eliminates hydrogen bonding to Arg 257. This finding underscores the importance of polar interactions in high-affinity binding to albumin.
-===HUMAN SERUM ALBUMIN COMPLEXED WITH IOPHENOXIC ACID===
+Crystallographic analysis reveals the structural basis of the high-affinity binding of Iophenoxic acid to Human Serum Albumin.,Ryan AJ, Chung CW, Curry S BMC Struct Biol. 2011 Apr 18;11(1):18. PMID:21501503<ref>PMID:21501503</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ydf" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21501503}}, adds the Publication Abstract to the page
+*[[Albumin 3D structures|Albumin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21501503 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21501503}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[2ydf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDF OCA].
-==Reference==
-<ref group="xtra">PMID:21501503</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Curry, S.]]
+[[Category: Large Structures]]
-[[Category: Ryan, A J.]]
+[[Category: Curry S]]
+[[Category: Ryan AJ]]