TY - JOUR
T1 - Structural and immunologic characterization of bovine, horse, and rabbit serum albumins
AU - Majorek, Karolina A.
AU - Porebski, Przemyslaw J.
AU - Dayal, Arjun
AU - Zimmerman, Matthew D.
AU - Jablonska, Kamila
AU - Stewart, Alan J.
AU - Chruszcz, Maksymilian
AU - Minor, Wladek
N1 - This article is highlighted in Nature's Structural Biology Knowledgebase (see http://www.sbkb.org/update/2012/08/full/sbkb.2011.91.html).
PY - 2012/10/1
Y1 - 2012/10/1
N2 - 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.
AB - 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.
UR - http://www.sciencedirect.com/science/article/pii/S0161589012002842
U2 - 10.1016/j.molimm.2012.05.011
DO - 10.1016/j.molimm.2012.05.011
M3 - Article
SN - 0161-5890
VL - 52
SP - 174
EP - 182
JO - Molecular Immunology
JF - Molecular Immunology
IS - 3-4
ER -