3lu7: Difference between revisions
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==Human serum albumin in complex with compound 2== | ==Human serum albumin in complex with compound 2== | ||
<StructureSection load='3lu7' size='340' side='right' caption='[[3lu7]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3lu7' size='340' side='right'caption='[[3lu7]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3lu7]] 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=3LU7 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[3lu7]] 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=3LU7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3LU7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPX:4-[(1R,2R)-2-{[(5-FLUORO-1H-INDOL-2-YL)CARBONYL]AMINO}-2,3-DIHYDRO-1H-INDEN-1-YL]BUTANOIC+ACID'>IPX</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPX:4-[(1R,2R)-2-{[(5-FLUORO-1H-INDOL-2-YL)CARBONYL]AMINO}-2,3-DIHYDRO-1H-INDEN-1-YL]BUTANOIC+ACID'>IPX</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lu6|3lu6]], [[3lu8|3lu8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lu6|3lu6]], [[3lu8|3lu8]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3lu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lu7 OCA], [http://pdbe.org/3lu7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lu7 RCSB], [http://www.ebi.ac.uk/pdbsum/3lu7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lu7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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==See Also== | ==See Also== | ||
*[[Albumin|Albumin]] | *[[Albumin 3D structures|Albumin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | |||
[[Category: Buttar, D]] | [[Category: Buttar, D]] | ||
[[Category: Colclough, N]] | [[Category: Colclough, N]] | ||
Revision as of 09:38, 14 October 2020
Human serum albumin in complex with compound 2Human serum albumin in complex with compound 2
Structural highlights
Disease[ALBU_HUMAN] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM: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.[1] [2] [3] [4] Function[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.[5] Publication Abstract from PubMedThe displacement of probes that bind selectively to subdomains IIA or IIIA on human serum albumin (HSA) by competing compounds has been followed using fluorescence spectroscopy, and has therefore been used to assign a primary binding site for these compounds in the presence and absence of fatty acids. The crystal structures have also been solved for three compounds: a matched pair of carboxylic acids whose binding strength to HSA unexpectedly decreased as the lipophilicity increased; and a highly bound sulphonamide that appeared not to displace the probes in the displacement assay. The crystallography results support the findings from the fluorescence displacement assay. The results indicate that drug binding to subdomain IB might also be important location for certain compounds. A combined spectroscopic and crystallographic approach to probing drug-human serum albumin interactions.,Buttar D, Colclough N, Gerhardt S, MacFaul PA, Phillips SD, Plowright A, Whittamore P, Tam K, Maskos K, Steinbacher S, Steuber H Bioorg Med Chem. 2010 Nov 1;18(21):7486-96. Epub 2010 Sep 24. PMID:20869876[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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