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== | ==Human serum albumin in complex with compound 2== | ||
[[http://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN | <StructureSection load='3lu7' size='340' side='right'caption='[[3lu7]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3lu7]] 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=3LU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LU7 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]] 2.8Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lu7 OCA], [https://pdbe.org/3lu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lu7 RCSB], [https://www.ebi.ac.uk/pdbsum/3lu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lu7 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 == | |||
The 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<ref>PMID:20869876</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3lu7" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Albumin|Albumin]] | *[[Albumin 3D structures|Albumin 3D structures]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Buttar | [[Category: Large Structures]] | ||
[[Category: Colclough | [[Category: Buttar D]] | ||
[[Category: Gerhardt | [[Category: Colclough N]] | ||
[[Category: MacFaul | [[Category: Gerhardt S]] | ||
[[Category: Maskos | [[Category: MacFaul PA]] | ||
[[Category: Phillips | [[Category: Maskos K]] | ||
[[Category: Plowright | [[Category: Phillips SD]] | ||
[[Category: Steinbacher | [[Category: Plowright A]] | ||
[[Category: Steuber | [[Category: Steinbacher S]] | ||
[[Category: Tam | [[Category: Steuber H]] | ||
[[Category: Whittamore | [[Category: Tam K]] | ||
[[Category: Whittamore P]] | |||
Latest revision as of 13:08, 6 November 2024
Human serum albumin in complex with compound 2Human serum albumin in complex with compound 2
Structural highlights
DiseaseALBU_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] FunctionALBU_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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