PMID- 18332182
OWN - NLM
STAT- MEDLINE
DCOM- 20080403
LR  - 20231213
IS  - 1540-9538 (Electronic)
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 205
IP  - 3
DP  - 2008 Mar 17
TI  - CD94-NKG2A recognition of human leukocyte antigen (HLA)-E bound to an HLA class I 
      leader sequence.
PG  - 725-35
LID - 10.1084/jem.20072525 [doi]
AB  - The recognition of human leukocyte antigen (HLA)-E by the heterodimeric CD94-NKG2 
      natural killer (NK) receptor family is a central innate mechanism by which NK 
      cells monitor the expression of other HLA molecules, yet the structural basis of 
      this highly specific interaction is unclear. Here, we describe the crystal 
      structure of CD94-NKG2A in complex with HLA-E bound to a peptide derived from the 
      leader sequence of HLA-G. The CD94 subunit dominated the interaction with HLA-E, 
      whereas the NKG2A subunit was more peripheral to the interface. Moreover, the 
      invariant CD94 subunit dominated the peptide-mediated contacts, albeit with poor 
      surface and chemical complementarity. This unusual binding mode was consistent 
      with mutagenesis data at the CD94-NKG2A-HLA-E interface. There were few 
      conformational changes in either CD94-NKG2A or HLA-E upon ligation, and such a 
      "lock and key" interaction is typical of innate receptor-ligand interactions. 
      Nevertheless, the structure also provided insight into how this interaction can 
      be modulated by subtle changes in the peptide ligand or by the pairing of CD94 
      with other members of the NKG2 family. Differences in the docking strategies used 
      by the NKG2D and CD94-NKG2A receptors provided a basis for understanding the 
      promiscuous nature of ligand recognition by NKG2D compared with the fidelity of 
      the CD94-NKG2 receptors.
FAU - Petrie, Emma J
AU  - Petrie EJ
AD  - The Protein Crystallography Unit, ARC Centre of Excellence in Structural and 
      Functional Microbial Genomics, Department of Biochemistry and Molecular Biology, 
      School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, 
      Australia.
FAU - Clements, Craig S
AU  - Clements CS
FAU - Lin, Jie
AU  - Lin J
FAU - Sullivan, Lucy C
AU  - Sullivan LC
FAU - Johnson, Darryl
AU  - Johnson D
FAU - Huyton, Trevor
AU  - Huyton T
FAU - Heroux, Annie
AU  - Heroux A
FAU - Hoare, Hilary L
AU  - Hoare HL
FAU - Beddoe, Travis
AU  - Beddoe T
FAU - Reid, Hugh H
AU  - Reid HH
FAU - Wilce, Matthew C J
AU  - Wilce MC
FAU - Brooks, Andrew G
AU  - Brooks AG
FAU - Rossjohn, Jamie
AU  - Rossjohn J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080310
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (HLA Antigens)
RN  - 0 (HLA-G Antigens)
RN  - 0 (Histocompatibility Antigens Class I)
RN  - 0 (KLRC1 protein, human)
RN  - 0 (KLRD1 protein, human)
RN  - 0 (KLRK1 protein, human)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (NK Cell Lectin-Like Receptor Subfamily C)
RN  - 0 (NK Cell Lectin-Like Receptor Subfamily D)
RN  - 0 (NK Cell Lectin-Like Receptor Subfamily K)
RN  - 0 (Protein Sorting Signals)
RN  - 0 (Protein Subunits)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Receptors, Natural Killer Cell)
RN  - 0 (Recombinant Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Crystallography, X-Ray
MH  - HLA Antigens/chemistry/genetics/*metabolism
MH  - HLA-G Antigens
MH  - Histocompatibility Antigens Class I/chemistry/genetics/*metabolism
MH  - Humans
MH  - In Vitro Techniques
MH  - Models, Molecular
MH  - Multiprotein Complexes
MH  - NK Cell Lectin-Like Receptor Subfamily C
MH  - NK Cell Lectin-Like Receptor Subfamily D/chemistry/genetics/*metabolism
MH  - NK Cell Lectin-Like Receptor Subfamily K
MH  - Protein Binding
MH  - Protein Sorting Signals/genetics
MH  - Protein Subunits
MH  - Receptors, Immunologic/chemistry/genetics/*metabolism
MH  - Receptors, Natural Killer Cell
MH  - Recombinant Proteins/chemistry/genetics/metabolism
MH  - Static Electricity
MH  - HLA-E Antigens
PMC - PMC2275392
EDAT- 2008/03/12 09:00
MHDA- 2008/04/04 09:00
PMCR- 2008/09/17
CRDT- 2008/03/12 09:00
PHST- 2008/03/12 09:00 [pubmed]
PHST- 2008/04/04 09:00 [medline]
PHST- 2008/03/12 09:00 [entrez]
PHST- 2008/09/17 00:00 [pmc-release]
AID - jem.20072525 [pii]
AID - 20072525 [pii]
AID - 10.1084/jem.20072525 [doi]
PST - ppublish
SO  - J Exp Med. 2008 Mar 17;205(3):725-35. doi: 10.1084/jem.20072525. Epub 2008 Mar 
      10.