4J2V

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

4J2V の概要

• エントリーDOI: 10.2210/pdb4j2v/pdb
• 関連するPDBエントリー: 4F5S 4F5T 4F5U 4JK4
• 分子名称: Serum albumin, 2-HYDROXY-3,5-DIIODO-BENZOIC ACID, MALONATE ION, ... (6 entities in total)
• 機能のキーワード: equine serum albumin, transport protein, helical, serum albumin superfamily, transport, fatty acids, metabolites and drugs, plasma
• 由来する生物種: Equus caballus (domestic horse,equine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68555.42

構造登録者

Sekula, B.,Bujacz, A.,Zielinski, K.,Bujacz, G. (登録日: 2013-02-05, 公開日: 2013-07-24, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.12 Å)