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PDBsum entry 3bdw

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protein Protein-protein interface(s) links
Immune system receptor PDB id
3bdw

 

 

 

 

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Contents
Protein chains
123 a.a. *
116 a.a. *
Waters ×51
* Residue conservation analysis
PDB id:
3bdw
Name: Immune system receptor
Title: Human cd94/nkg2a
Structure: Natural killer cells antigen cd94. Chain: a, c. Fragment: residues unp 57-179. Synonym: nk cell receptor, killer cell lectin-like receptor subfamily d member 1, kp43. Engineered: yes. Nkg2-a/nkg2-b type ii integral membrane protein. Chain: b, d. Fragment: residues unp 113-232.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: klrd1, cd94. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: klrc1, nkg2a.
Resolution:
2.50Å     R-factor:   0.236     R-free:   0.270
Authors: L.C.Sullivan,C.S.Clements
Key ref: L.C.Sullivan et al. (2007). The heterodimeric assembly of the CD94-NKG2 receptor family and implications for human leukocyte antigen-E recognition. Immunity, 27, 900-911. PubMed id: 18083576
Date:
15-Nov-07     Release date:   01-Jan-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q13241  (KLRD1_HUMAN) -  Natural killer cells antigen CD94 from Homo sapiens
Seq:
Struc:
179 a.a.
123 a.a.
Protein chains
Pfam   ArchSchema ?
P26715  (NKG2A_HUMAN) -  NKG2-A/NKG2-B type II integral membrane protein from Homo sapiens
Seq:
Struc:
233 a.a.
116 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Immunity 27:900-911 (2007)
PubMed id: 18083576  
 
 
The heterodimeric assembly of the CD94-NKG2 receptor family and implications for human leukocyte antigen-E recognition.
L.C.Sullivan, C.S.Clements, T.Beddoe, D.Johnson, H.L.Hoare, J.Lin, T.Huyton, E.J.Hopkins, H.H.Reid, M.C.Wilce, J.Kabat, F.Borrego, J.E.Coligan, J.Rossjohn, A.G.Brooks.
 
  ABSTRACT  
 
The CD94-NKG2 receptor family that regulates NK and T cells is unique among the lectin-like receptors encoded within the natural killer cell complex. The function of the CD94-NKG2 receptors is dictated by the pairing of the invariant CD94 polypeptide with specific NKG2 isoforms to form a family of functionally distinct heterodimeric receptors. However, the structural basis for this selective pairing and how they interact with their ligand, HLA-E, is unknown. We describe the 2.5 A resolution crystal structure of CD94-NKG2A in which the mode of dimerization contrasts with that of other homodimeric NK receptors. Despite structural homology between the CD94 and NKG2A subunits, the dimer interface is asymmetric, thereby providing a structural basis for the preferred heterodimeric assembly. Structure-based sequence comparisons of other CD94-NKG2 family members, combined with extensive mutagenesis studies on HLA-E and CD94-NKG2A, allows a model of the interaction between CD94-NKG2A and HLA-E to be established, in which the invariant CD94 chain plays a more dominant role in interacting with HLA-E in comparison to the variable NKG2 chain.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21212510 K.Higai, C.Suzuki, Y.Imaizumi, X.Xin, Y.Azuma, and K.Matsumoto (2011).
Binding affinities of NKG2D and CD94 to sialyl Lewis X-expressing N-glycans and heparin.
  Biol Pharm Bull, 34, 8.  
21135867 T.Beddoe, A.G.Brooks, and J.Rossjohn (2011).
How opposites attract.
  Immunol Cell Biol, 89, 163-164.  
21467632 X.Xin, K.Higai, Y.Imaizumi, C.Suzuki, K.Ito, A.Itoh, S.Matsumoto, Y.Azuma, and K.Matsumoto (2011).
Natural killer group 2A (NKG2A) and natural killer group 2C (NKG2C) bind to sulfated glycans and α2,3-NeuAc-containing glycoproteins.
  Biol Pharm Bull, 34, 480-485.  
20133787 J.W.Leavenworth, C.Schellack, H.J.Kim, L.Lu, P.Spee, and H.Cantor (2010).
Analysis of the cellular mechanism underlying inhibition of EAE after treatment with anti-NKG2A F(ab')2.
  Proc Natl Acad Sci U S A, 107, 2562-2567.  
21134635 M.E.Call, and J.J.Chou (2010).
A view into the blind spot: solution NMR provides new insights into signal transduction across the lipid bilayer.
  Structure, 18, 1559-1569.  
21151939 M.T.Orr, J.Wu, M.Fang, L.J.Sigal, P.Spee, T.Egebjerg, E.Dissen, S.Fossum, J.H.Phillips, and L.L.Lanier (2010).
Development and function of CD94-deficient natural killer cells.
  PLoS One, 5, e15184.  
20122941 N.G.Walpole, L.Kjer-Nielsen, L.Kostenko, J.McCluskey, A.G.Brooks, J.Rossjohn, and C.S.Clements (2010).
The structure and stability of the monomorphic HLA-G are influenced by the nature of the bound peptide.
  J Mol Biol, 397, 467-480.
PDB codes: 3kyn 3kyo
20195281 T.H.Nguyen, L.C.Sullivan, T.C.Kotsimbos, A.P.Schwarer, and N.A.Mifsud (2010).
Cross-presentation of HCMV chimeric protein enables generation and measurement of polyclonal T cells.
  Immunol Cell Biol, 88, 676-684.  
18448674 B.K.Kaiser, J.C.Pizarro, J.Kerns, and R.K.Strong (2008).
Structural basis for NKG2A/CD94 recognition of HLA-E.
  Proc Natl Acad Sci U S A, 105, 6696-6701.
PDB code: 3cii
18332182 E.J.Petrie, C.S.Clements, J.Lin, L.C.Sullivan, D.Johnson, T.Huyton, A.Heroux, H.L.Hoare, T.Beddoe, H.H.Reid, M.C.Wilce, A.G.Brooks, and J.Rossjohn (2008).
CD94-NKG2A recognition of human leukocyte antigen (HLA)-E bound to an HLA class I leader sequence.
  J Exp Med, 205, 725-735.
PDB code: 3cdg
18946929 L.C.Sullivan, C.S.Clements, J.Rossjohn, and A.G.Brooks (2008).
The major histocompatibility complex class Ib molecule HLA-E at the interface between innate and adaptive immunity.
  Tissue Antigens, 72, 415-424.  
18574582 S.L.Rogers, and J.Kaufman (2008).
High allelic polymorphism, moderate sequence diversity and diversifying selection for B-NK but not B-lec, the pair of lectin-like receptor genes in the chicken MHC.
  Immunogenetics, 60, 461-475.  
18309314 W.Held, and R.A.Mariuzza (2008).
Cis interactions of immunoreceptors with MHC and non-MHC ligands.
  Nat Rev Immunol, 8, 269-278.  
18439809 Y.T.Bryceson, and E.O.Long (2008).
Line of attack: NK cell specificity and integration of signals.
  Curr Opin Immunol, 20, 344-352.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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