8VAF
Cryogenic electron microscopy structure of apo human serum albumin
Summary for 8VAF
| Entry DOI | 10.2210/pdb8vaf/pdb |
| EMDB information | 43090 |
| Descriptor | Serum albumin (1 entity in total) |
| Functional Keywords | human serum albumin, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 66571.22 |
| Authors | Catalano, C.,Lucier, K.W.,To, D.,Senko, S.,Tran, N.L.,Farwell, A.C.,Silva, S.M.,Dip, P.V.,Poweleit, N.,Scapin, G. (deposition date: 2023-12-11, release date: 2024-06-26, Last modification date: 2024-10-30) |
| Primary citation | Catalano, C.,Lucier, K.W.,To, D.,Senko, S.,Tran, N.L.,Farwell, A.C.,Silva, S.M.,Dip, P.V.,Poweleit, N.,Scapin, G. The CryoEM structure of human serum albumin in complex with ligands. J.Struct.Biol., 216:108105-108105, 2024 Cited by PubMed Abstract: 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 Å, respectively. We expand upon previously published work and further demonstrate that sub-4 Å maps of ∼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. PubMed: 38852682DOI: 10.1016/j.jsb.2024.108105 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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