8vaf
Cryogenic electron microscopy structure of apo human serum albumin
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 PubMedHuman 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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