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PDBsum entry 3v09
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Transport protein
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PDB id
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3v09
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References listed in PDB file
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Key reference
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Title
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Structural and immunologic characterization of bovine, Horse, And rabbit serum albumins.
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Authors
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K.A.Majorek,
P.J.Porebski,
A.Dayal,
M.D.Zimmerman,
K.Jablonska,
A.J.Stewart,
M.Chruszcz,
W.Minor.
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Ref.
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Mol Immunol, 2012,
52,
174-182.
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PubMed id
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Abstract
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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) 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.
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