3V09

Crystal structure of Rabbit Serum Albumin

Summary for 3V09

• Entry DOI: 10.2210/pdb3v09/pdb
• Descriptor: Serum albumin, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, TETRAETHYLENE GLYCOL, ... (7 entities in total)
• Functional Keywords: allergen, structural genomics, psi-biology, new york structural genomics research consortium, nysgrc, carrier protein, transport protein
• Biological source: Oryctolagus cuniculus (European rabbit,Japanese white rabbit,domestic rabbit,rabbits)
• Cellular location: Secreted: P49065
• Total number of polymer chains: 1
• Total formula weight: 69705.01

Authors

Majorek, K.A.,Porebski, P.J.,Chruszcz, M.,Almo, S.C.,Minor, W.,New York Structural Genomics Research Consortium (NYSGRC) (deposition date: 2011-12-07, release date: 2012-01-18, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.27 Å)