8VAE

Cryogenic electron microscopy structure of human serum albumin in complex with salicylic acid

Summary for 8VAE

• Entry DOI: 10.2210/pdb8vae/pdb
• EMDB information: 43089
• Descriptor: Serum albumin, 2-HYDROXYBENZOIC ACID (2 entities in total)
• Functional Keywords: human serum albumin, salicylic acid, transport protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 66985.58

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: 2024-10-16)

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

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: 38852682
DOI: 10.1016/j.jsb.2024.108105

Experimental method

ELECTRON MICROSCOPY (3.7 Å)