4JK4

Crystal Structure of Bovine Serum Albumin in complex with 3,5-diiodosalicylic acid

Summary for 4JK4

• Entry DOI: 10.2210/pdb4jk4/pdb
• Related: 4F5S 4F5T 4F5U 4J2V
• Descriptor: Serum albumin, 2-HYDROXY-3,5-DIIODO-BENZOIC ACID, DI(HYDROXYETHYL)ETHER, ... (7 entities in total)
• Functional Keywords: bovine serum albumin, transport protein, helical protein possessing three domains, transport, fatty acids, hormones, metabolites and drugs, plasma
• Biological source: Bos taurus (bovine)
• Total number of polymer chains: 2
• Total formula weight: 137751.22

Authors

Zielinski, K.,Bujacz, A.,Sekula, B.,Bujacz, G. (deposition date: 2013-03-09, release date: 2013-07-24, Last modification date: 2024-10-30)

Primary citation

Sekula, B.,Zielinski, K.,Bujacz, A.
Crystallographic studies of the complexes of bovine and equine serum albumin with 3,5-diiodosalicylic acid.
Int.J.Biol.Macromol., 60C:316-324, 2013

PubMed Abstract: Due to their extraordinary binding properties, serum albumins are the main transporters of many small molecules in the circulatory system. Although all mammalian serum albumins exhibit quite high sequence similarity, their binding abilities are not the same. Until now, only human serum albumin (HSA) was subjected to extensive structural studies in complexes with various ligands. Here we present two crystal structures of the complexes of equine and bovine serum albumins with 3,5-diiodosalicylic acid (DIS), at resolutions 2.12 Å and 2.65 Å, respectively, and analyze interactions of the DIS ligand with both macromolecules. We highlight the differences in distribution of DIS binding sites between the bovine and equine serum albumins and compare results with the HSA binding ability of DIS and other structurally similar ligands.

PubMed: 23769932
DOI: 10.1016/j.ijbiomac.2013.06.004

Experimental method

X-RAY DIFFRACTION (2.653 Å)