Structural and immunologic characterization of bovine, horse, and rabbit serum albumins
By K. Majorek, Przemyslaw J. Porebski, A. Dayal, Matthew D. Zimmerman, K. Jabłońska, Alan J. Stewart, M. Chruszcz, Wladek Minor. Molecular Immunology, 2012
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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) serums. 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.
Subfields: Molecular Biology, Pulmonary and Respiratory Medicine
View Paper: https://www.semanticscholar.org/paper/f25dc5b67e67bce859cd443fa86bbd645ca8fb14
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In Molecular Biology
Citations in the corpus
- Structures of bovine, equine and leporine serum albumin. (2012, background): “Note added in proof: While this paper was under review, an independent publication describing structural studies of bovine, horse and rabbit albumins became available (Majorek et al., 2012).”