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PDBsum entry 3g8l

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protein Protein-protein interface(s) links
Immune system PDB id
3g8l
Jmol
Contents
Protein chains
157 a.a. *
Waters ×17
* Residue conservation analysis
PDB id:
3g8l
Name: Immune system
Title: Crystal structure of murine natural killer cell receptor, ly49l4
Structure: Lectin-related nk cell receptor ly49l1. Chain: a, b, c, d. Fragment: c-type lectin-like domain with a part of the stalk (unp residues 80-281). Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: klra12, mouse. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.228     R-free:   0.287
Authors: S.Cho
Key ref: J.Back et al. (2009). Distinct conformations of Ly49 natural killer cell receptors mediate MHC class I recognition in trans and cis. Immunity, 31, 598-608. PubMed id: 19818651
Date:
12-Feb-09     Release date:   17-Nov-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9JIP9  (Q9JIP9_MOUSE) -  Lectin-related NK cell receptor LY49L4
Seq:
Struc:
265 a.a.
157 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     carbohydrate binding     1 term  

 

 
Immunity 31:598-608 (2009)
PubMed id: 19818651  
 
 
Distinct conformations of Ly49 natural killer cell receptors mediate MHC class I recognition in trans and cis.
J.Back, E.L.Malchiodi, S.Cho, L.Scarpellino, P.Schneider, M.C.Kerzic, R.A.Mariuzza, W.Held.
 
  ABSTRACT  
 
Certain cell-surface receptors engage ligands expressed on juxtaposed cells and ligands on the same cell. The structural basis for trans versus cis binding is not known. Here, we showed that Ly49 natural killer (NK) cell receptors bound two MHC class I (MHC-I) molecules in trans when the two ligand-binding domains were backfolded onto the long stalk region. In contrast, dissociation of the ligand-binding domains from the stalk and their reorientation relative to the NK cell membrane allowed monovalent binding of MHC-I in cis. The distinct conformations (backfolded and extended) define the structural basis for cis-trans binding by Ly49 receptors and explain the divergent functional consequences of cis versus trans interactions. Further analyses identified specific stalk segments that were not required for MHC-I binding in trans but were essential for inhibitory receptor function. These data identify multiple distinct roles of stalk regions for receptor function.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20976309 T.Takai, A.Nakamura, and S.Endo (2011).
Role of PIR-B in autoimmune glomerulonephritis.
  J Biomed Biotechnol, 2011, 275302.  
21159498 W.Held, M.Kijima, G.Angelov, and S.Bessoles (2011).
The function of natural killer cells: education, reminders and some good memories.
  Curr Opin Immunol, 23, 228-233.  
20952682 M.H.Brown, and E.Lacey (2010).
A ligand for CD5 is CD5.
  J Immunol, 185, 6068-6074.  
  20957233 P.Brodin, T.Lakshmikanth, R.Mehr, M.H.Johansson, A.D.Duru, A.Achour, M.Salmon-Divon, K.Kärre, P.Höglund, and S.Johansson (2010).
Natural killer cell tolerance persists despite significant reduction of self MHC class I on normal target cells in mice.
  PLoS One, 5, 0.  
20818413 P.Höglund, and P.Brodin (2010).
Current perspectives of natural killer cell education by MHC class I molecules.
  Nat Rev Immunol, 10, 724-734.  
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.