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PDBsum entry 4f7c

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protein ligands Protein-protein interface(s) links
Immune system PDB id
4f7c

 

 

 

 

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Contents
Protein chains
269 a.a.
97 a.a.
Ligands
NAG-NAG
NAG-NAG-BMA ×2
NAG-NAG-BMA-BMA
0SG ×2
Waters ×29
PDB id:
4f7c
Name: Immune system
Title: Crystal structure of bovine cd1d with bound c12-di-sulfatide
Structure: Cd1d antigen, d polypeptide. Chain: a, c. Fragment: unp residues 129-405. Synonym: t cell surface glycoprotein cd1d antigen. Engineered: yes. Beta-2-microglobulin. Chain: b, d. Fragment: unp residues 21-118. Synonym: lactollin.
Source: Bos taurus. Bovine. Organism_taxid: 9913. Gene: cd1d. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: b2m.
Resolution:
2.86Å     R-factor:   0.225     R-free:   0.291
Authors: J.Wang,D.M.Zajonc
Key ref: J.Wang et al. (2012). Crystal structures of bovine CD1d reveal altered αGalCer presentation and a restricted A' pocket unable to bind long-chain glycolipids. Plos One, 7, e47989. PubMed id: 23110152
Date:
15-May-12     Release date:   14-Nov-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A1L565  (A1L565_BOVIN) -  CD1D antigen, d polypeptide (Fragment) from Bos taurus
Seq:
Struc:
445 a.a.
269 a.a.*
Protein chains
Pfam   ArchSchema ?
P01888  (B2MG_BOVIN) -  Beta-2-microglobulin from Bos taurus
Seq:
Struc:
118 a.a.
97 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
Plos One 7:e47989 (2012)
PubMed id: 23110152  
 
 
Crystal structures of bovine CD1d reveal altered αGalCer presentation and a restricted A' pocket unable to bind long-chain glycolipids.
J.Wang, J.Guillaume, N.Pauwels, S.Van Calenbergh, I.Van Rhijn, D.M.Zajonc.
 
  ABSTRACT  
 
NKT cells play important roles in immune surveillance. They rapidly respond to pathogens by detecting microbial glycolipids when presented by the non-classical MHC I homolog CD1d. Previously, ruminants were considered to lack NKT cells due to the lack of a functional CD1D gene. However, recent data suggest that cattle express CD1d with unknown function. In an attempt to characterize the function of bovine CD1d, we assessed the lipid binding properties of recombinant Bos taurus CD1d (boCD1d) in vitro. BoCD1d is able to bind glycosphingolipids (GSLs) with fatty acid chain lengths of C(18), while GSLs with fatty acids of C(24) do not bind. Crystal structures of boCD1d bound to a short-chain C(12)-di-sulfatide antigen, as well as short-chain C(16)-αGalCer revealed that the Á pocket of boCD1d is restricted in size compared to that of both mouse and human CD1d, explaining the inability of long chain GSL's to bind to boCD1d. Moreover, while di-sulfatide is presented similarly compared to the presentation of sulfatide by mouse CD1d, αGalCer is presented differently at the cell surface, due to an amino acid Asp151Asn substitution that results in loss of intimate contacts between the αGalCer headgroup and CD1d. The altered αGalCer presentation by boCD1d also explains its lack of cross-activation of mouse iNKT cells and raises the interesting question of the nature and function of bovine lipid-reactive T cells.
 

 

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