3V08

Crystal structure of Equine Serum Albumin

3V08 の概要

• エントリーDOI: 10.2210/pdb3v08/pdb
• 分子名称: Serum albumin, BROMIDE ION, SULFATE ION, ... (7 entities in total)
• 機能のキーワード: allergen, structural genomics, psi-biology, new york structural genomics research consortium, nysgrc, carrier protein, transport protein
• 由来する生物種: Equus caballus (domestic horse,equine)
• 細胞内の位置: Secreted: P35747
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67565.82

構造登録者

Dayal, A.,Jablonska, K.,Porebski, P.J.,Majorek, K.A.,Chruszcz, M.,Almo, S.C.,Minor, W.,New York Structural Genomics Research Consortium (NYSGRC) (登録日: 2011-12-07, 公開日: 2012-01-11, 最終更新日: 2024-11-20)

主引用文献

Majorek, K.A.,Porebski, P.J.,Dayal, A.,Zimmerman, M.D.,Jablonska, K.,Stewart, A.J.,Chruszcz, M.,Minor, W.
Structural and immunologic characterization of bovine, horse, and rabbit serum albumins.
Mol.Immunol., 52:174-182, 2012

PubMed Abstract: Serum albumin (SA) is the most abundant plasma protein in mammals. SA is a multifunctional protein with extraordinary ligand binding capacity, making it a transporter molecule for a diverse range of metabolites, drugs, nutrients, metals and other molecules. Due to its ligand binding properties, albumins have wide clinical, pharmaceutical, and biochemical applications. Albumins are also allergenic, and exhibit a high degree of cross-reactivity due to significant sequence and structure similarity of SAs from different organisms. Here we present crystal structures of albumins from cattle (BSA), horse (ESA) and rabbit (RSA) sera. The structural data are correlated with the results of immunological studies of SAs. We also analyze the conservation or divergence of structures and sequences of SAs in the context of their potential allergenicity and cross-reactivity. In addition, we identified a previously uncharacterized ligand binding site in the structure of RSA, and calcium binding sites in the structure of BSA, which is the first serum albumin structure to contain metal ions.

PubMed: 22677715
DOI: 10.1016/j.molimm.2012.05.011

実験手法

X-RAY DIFFRACTION (2.45 Å)