2YDF

HUMAN SERUM ALBUMIN COMPLEXED WITH IOPHENOXIC ACID

Summary for 2YDF

• Entry DOI: 10.2210/pdb2ydf/pdb
• Related: 1AO6 1BJ5 1BKE 1BM0 1E78 1E7A 1E7B 1E7C 1E7E 1E7F 1E7G 1E7H 1E7I 1GNI 1GNJ 1H9Z 1HA2 1HK1 1HK2 1HK3 1HK4 1HK5 1N5U 1O9X 1TF0 1UOR 1YSX 2BX8 2BXA 2BXB 2BXC 2BXD 2BXE 2BXF 2BXG 2BXH 2BXI 2BXK 2BXL 2BXM 2BXN 2BXO 2BXP 2BXQ 2ESG 2VDB 2VUE 2VUF 2XSI 2XVQ 2XVU 2XVV 2XVW 2XW0 2XW1
• Descriptor: SERUM ALBUMIN, IOPHENOXIC ACID (3 entities in total)
• Functional Keywords: transport protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Secreted: P02768
• Total number of polymer chains: 2
• Total formula weight: 137717.77

Authors

Ryan, A.J.,Curry, S. (deposition date: 2011-03-18, release date: 2011-04-27, Last modification date: 2024-11-20)

Primary citation

Ryan, A.J.,Chung, C.W.,Curry, S.
Crystallographic Analysis Reveals the Structural Basis of the High-Affinity Binding of Iophenoxic Acid to Human Serum Albumin.
Bmc Struct.Biol., 11:18-, 2011

PubMed Abstract: Iophenoxic acid is an iodinated radiocontrast agent that was withdrawn from clinical use because of its exceptionally long half-life in the body, which was due in part to its high-affinity binding to human serum albumin (HSA). It was replaced by Iopanoic acid, which has an amino rather than a hydroxyl group at position 3 on the iodinated benzyl ring and, as a result, binds to albumin with lower affinity and is excreted more rapidly from the body. To understand how iophenoxic acid binds so tightly to albumin, we wanted to examine the structural basis of its interaction with HSA.

PubMed: 21501503
DOI: 10.1186/1472-6807-11-18

Experimental method

X-RAY DIFFRACTION (2.75 Å)