2VDB

Structure of human serum albumin with S-naproxen and the GA module

Summary for 2VDB

• Entry DOI: 10.2210/pdb2vdb/pdb
• Related: 1AO6 1BJ5 1BKE 1BM0 1E78 1E7A 1E7B 1E7C 1E7E 1E7F 1E7G 1E7H 1E7I 1GAB 1GNI 1GNJ 1H9Z 1HA2 1HK1 1HK2 1HK3 1HK4 1HK5 1N5U 1O9X 1PRB 1TF0 1UOR 1YSX 2BX8 2BXA 2BXB 2BXC 2BXD 2BXE 2BXF 2BXG 2BXH 2BXI 2BXK 2BXL 2BXM 2BXN 2BXO 2BXP 2BXQ 2ESG 2J5Y
• Descriptor: SERUM ALBUMIN, PEPTOSTREPTOCOCCAL ALBUMIN-BINDING PROTEIN, DECANOIC ACID, ... (4 entities in total)
• Functional Keywords: lipid-binding, metal-binding, protein binding, peptidoglycan-anchor, bacterial albumin-binding, disease mutation, three-helix bundle, ga module, drug binding, glycoprotein, cleavage on pair of basic residues, human serum albumin, secreted, naproxen, cell wall, glycation
• Biological source: PEPTOSTREPTOCOCCUS MAGNUS; More
• Cellular location: Secreted: P02768; Secreted, cell wall; Peptidoglycan-anchor (Potential): Q51911
• Total number of polymer chains: 2
• Total formula weight: 73390.46

Authors

Lejon, S.,Cramer, J.F.,Nordberg, P.A. (deposition date: 2007-10-04, release date: 2008-02-26, Last modification date: 2024-10-23)

Primary citation

Lejon, S.,Cramer, J.F.,Nordberg, P.A.
Structural Basis for the Binding of Naproxen to Human Serum Albumin in the Presence of Fatty Acids and the Ga Module.
Acta Crystallogr.,Sect.F, 64:64-, 2008

PubMed Abstract: The previously determined crystal structure of the bacterial albumin-binding GA module in complex with human serum albumin (HSA) suggested the possibility of utilizing the complex in the study of ligand binding to HSA. As a continuation of these studies, the crystal structure of the HSA-GA complex with the drug molecule naproxen and the fatty acid decanoate bound to HSA has been determined to a resolution of 2.5 A. In terms of drug binding, the structure suggests that the binding of decanoate to the albumin molecule may play a role in making the haemin site in subdomain IB of the albumin molecule available for the binding of naproxen. In addition, structure comparisons with solved structures of HSA and of the HSA-GA complex show that the GA module is capable of binding to different conformations of HSA. The HSA-GA complex therefore emerges as a possible platform for the crystallographic study of specific HSA-drug interactions and of the influence exerted by the presence of fatty acids.

PubMed: 18259051
DOI: 10.1107/S174430910706770X

Experimental method

X-RAY DIFFRACTION (2.52 Å)