View source for 8vaf


==Cryogenic electron microscopy structure of apo human serum albumin==
<StructureSection load='8vaf' size='340' side='right'caption='[[8vaf]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8vaf]] 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=8VAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VAF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</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=8vaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vaf OCA], [https://pdbe.org/8vaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vaf RCSB], [https://www.ebi.ac.uk/pdbsum/8vaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vaf 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 ==
Human serum albumin (HSA) is the most prevalent plasma protein in the human body, accounting for 60 % of the total plasma protein. HSA plays a major pharmacokinetic function, serving as a facilitator in the distribution of endobiotics and xenobiotics within the organism. In this paper we report the cryoEM structures of HSA in the apo form and in complex with two ligands (salicylic acid and teniposide) at a resolution of 3.5, 3.7 and 3.4 A, respectively. We expand upon previously published work and further demonstrate that sub-4 A maps of approximately 60 kDa proteins can be routinely obtained using a 200 kV microscope, employing standard workflows. Most importantly, these maps allowed for the identification of small molecule ligands, emphasizing the practical applicability of this methodology and providing a starting point for subsequent computational modeling and in silico optimization.

The CryoEM structure of human serum albumin in complex with ligands.,Catalano C, Lucier KW, To D, Senko S, Tran NL, Farwell AC, Silva SM, Dip PV, Poweleit N, Scapin G J Struct Biol. 2024 Sep;216(3):108105. doi: 10.1016/j.jsb.2024.108105. Epub 2024 , Jun 8. PMID:38852682<ref>PMID:38852682</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8vaf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Catalano C]]
[[Category: Dip PV]]
[[Category: Farwell AC]]
[[Category: Lucier KW]]
[[Category: Poweleit N]]
[[Category: Scapin G]]
[[Category: Senko S]]
[[Category: Silva SM]]
[[Category: To D]]
[[Category: Tran NL]]