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PDBsum entry 3v09

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protein ligands metals links
Transport protein PDB id
3v09

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
583 a.a.
Ligands
MES ×2
PG4 ×3
UNX-UNX-UNX-UNX-
UNX-UNX-UNX-UNX-
UNX-UNX-UNX-UNX-
UNX-UNX-UNX-UNX-
UNX-UNX-UNX-UNX-
UNX-UNX
EDO ×5
Metals
_CL
Waters ×187
PDB id:
3v09
Name: Transport protein
Title: Crystal structure of rabbit serum albumin
Structure: Serum albumin. Chain: a
Source: Oryctolagus cuniculus. European rabbit,japanese white rabbit,domestic rabbit,rabbits. Organism_taxid: 9986
Resolution:
2.27Å     R-factor:   0.195     R-free:   0.243
Authors: K.A.Majorek,P.J.Porebski,M.Chruszcz,S.C.Almo,W.Minor,New York Structural Genomics Research Consortium (Nysgrc)
Key ref: K.A.Majorek et al. (2012). Structural and immunologic characterization of bovine, horse, and rabbit serum albumins. Mol Immunol, 52, 174-182. PubMed id: 22677715
Date:
07-Dec-11     Release date:   18-Jan-12    
PROCHECK
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 Headers
 References

Protein chain
P49065  (ALBU_RABIT) -  Albumin from Oryctolagus cuniculus
Seq:
Struc:
 
Seq:
Struc:
608 a.a.
583 a.a.
Key:    Secondary structure  CATH domain

 

 
Mol Immunol 52:174-182 (2012)
PubMed id: 22677715  
 
 
Structural and immunologic characterization of bovine, horse, and rabbit serum albumins.
K.A.Majorek, P.J.Porebski, A.Dayal, M.D.Zimmerman, K.Jablonska, A.J.Stewart, M.Chruszcz, W.Minor.
 
  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.
 

 

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