Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9UPD

Crystal structure of human serum albumin complex with nateglinide

This is a non-PDB format compatible entry.
Summary for 9UPD
Entry DOI10.2210/pdb9upd/pdb
DescriptorSerum albumin, (2R)-3-phenyl-2-[(4-propan-2-ylcyclohexyl)carbonylamino]propanoic acid, PHOSPHATE ION (3 entities in total)
Functional Keywordshuman serum albumin, nateglinide, complex, transport protein
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight133967.23
Authors
Kawai, A.,Nishi, K.,Yamasaki, K. (deposition date: 2025-04-28, release date: 2025-07-16, Last modification date: 2025-09-03)
Primary citationKawai, A.,Nishi, K.,Tokuno, M.,Otagiri, M.,Yamasaki, K.
Insights into Dual Binding Modes of Nateglinide to Human Serum Albumin.
Acs Med.Chem.Lett., 16:1619-1625, 2025
Cited by
PubMed Abstract: Nateglinide is a short-acting insulin secretagogue clinically used for the treatment of type 2 diabetes mellitus. Nateglinide exhibits a high plasma protein binding rate of approximately 98%, primarily binding to subdomain IIIA of human serum albumin (HSA). Here, we determined the crystal structure of the HSA-nateglinide complex at 2.80 Å resolution, revealing dual binding modes of nateglinide within the same binding site. To evaluate the stability of these alternative binding modes, molecular dynamics simulations were conducted, and binding free energies were calculated using the molecular mechanics Poisson-Boltzmann surface area method. The calculated binding free energy values were consistent with experimentally determined data. Our results highlight the structural adaptability of HSA and emphasize the possibility of alternative ligand binding modes existing within a single binding site, as well as the importance of identifying and characterizing these modes to enhance our understanding of drug-plasma protein interactions.
PubMed: 40832515
DOI: 10.1021/acsmedchemlett.5c00277
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

243531

건을2025-10-22부터공개중

PDB statisticsPDBj update infoContact PDBjnumon