1e7f: Difference between revisions

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-[[Image:1e7f.jpg|left|200px]]<br /><applet load="1e7f" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1e7f, resolution 2.43&Aring;" />
-'''HUMAN SERUM ALBUMIN COMPLEXED WITH DODECANOIC ACID (LAURIC ACID)'''<br />
-==Overview==
+==HUMAN SERUM ALBUMIN COMPLEXED WITH DODECANOIC ACID (LAURIC ACID)==
-Human serum albumin (HSA) is an abundant plasma protein that is, responsible for the transport of fatty acids. HSA also binds and perturbs, the pharmacokinetics of a wide range of drug compounds. Binding studies, have revealed significant interactions between fatty acid and drug-binding, sites on albumin but high-resolution structural information on ligand, binding to the protein has been lacking. We report here a crystallographic, study of five HSA-fatty acid complexes formed using saturated medium-chain, and long-chain fatty acids (C10:0, C12:0, C14:0, C16:0 and C18:0). A total, of seven binding sites that are occupied by all medium-chain and, long-chain fatty acids have been identified, although medium-chain fatty, acids are found to bind at additional sites on the protein, yielding a, total of 11 distinct binding locations. Comparison of the different, complexes reveals key similarities and significant differences in the, modes of binding, and serves to rationalise much of the biochemical data, on fatty acid interactions with albumin. The two principal drug-binding, sites, in sub-domains IIA and IIIA, are observed to be occupied by fatty, acids and one of them (in IIIA) appears to coincide with a high-affinity, long-chain fatty acid binding site.
+<StructureSection load='1e7f' size='340' side='right'caption='[[1e7f]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1e7f]] is a 1 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=1E7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E7F 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]] 2.43&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAO:LAURIC+ACID'>DAO</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=1e7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7f OCA], [https://pdbe.org/1e7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e7f RCSB], [https://www.ebi.ac.uk/pdbsum/1e7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e7f 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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e7/1e7f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e7f ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Human serum albumin (HSA) is an abundant plasma protein that is responsible for the transport of fatty acids. HSA also binds and perturbs the pharmacokinetics of a wide range of drug compounds. Binding studies have revealed significant interactions between fatty acid and drug-binding sites on albumin but high-resolution structural information on ligand binding to the protein has been lacking. We report here a crystallographic study of five HSA-fatty acid complexes formed using saturated medium-chain and long-chain fatty acids (C10:0, C12:0, C14:0, C16:0 and C18:0). A total of seven binding sites that are occupied by all medium-chain and long-chain fatty acids have been identified, although medium-chain fatty acids are found to bind at additional sites on the protein, yielding a total of 11 distinct binding locations. Comparison of the different complexes reveals key similarities and significant differences in the modes of binding, and serves to rationalise much of the biochemical data on fatty acid interactions with albumin. The two principal drug-binding sites, in sub-domains IIA and IIIA, are observed to be occupied by fatty acids and one of them (in IIIA) appears to coincide with a high-affinity long-chain fatty acid binding site.
-==Disease==
+Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin.,Bhattacharya AA, Grune T, Curry S J Mol Biol. 2000 Nov 10;303(5):721-32. PMID:11061971<ref>PMID:11061971</ref>
-Known diseases associated with this structure: Analbuminemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]], Dysalbuminemic hyperthyroxinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]], Dysalbuminemic hyperzincemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]]
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-E7F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=DAO:'>DAO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7F OCA].
+</div>
+<div class="pdbe-citations 1e7f" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin., Bhattacharya AA, Grune T, Curry S, J Mol Biol. 2000 Nov 10;303(5):721-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11061971 11061971]
+*[[Albumin 3D structures|Albumin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bhattacharya, A.A.]]
+[[Category: Bhattacharya AA]]
-[[Category: Curry, S.]]
+[[Category: Curry S]]
-[[Category: Gruene, T.]]
+[[Category: Gruene T]]
-[[Category: DAO]]
-[[Category: lipid-binding]]
-[[Category: metal-binding]]
-[[Category: plasma protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:41:43 2008''