PMID- 9288975
OWN - NLM
STAT- MEDLINE
DCOM- 19970918
LR  - 20071115
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 389
IP  - 6646
DP  - 1997 Sep 4
TI  - Structure of the inhibitory receptor for human natural killer cells resembles 
      haematopoietic receptors.
PG  - 96-100
AB  - Abnormal cells deficient in class I major histocompatibility complex (MHC) 
      expression are lysed by a class of lymphocytes called natural killer (NK) cells. 
      This lysis provides a defence against pathogens and tumour cells that 
      downregulate MHC expression to avoid an MHC-restricted, T-cell immune response. 
      Normal cells escape lysis because their MHC molecules are recognized by NK-cell 
      inhibitory receptors, which inhibit lysis. Several such inhibitory receptor 
      families have been described in humans and mice. In the human killer-cell 
      inhibitory receptor family, individual p58 members are specific for a subset of 
      class I human leukocyte antigen (HLA)-C molecules. The human p58 natural 
      killer-cell inhibitory receptor clone 42 recognizes HLA-Cw4, -Cw2 and -Cw6, but 
      not HLA-Cw3, -Cw2, -Cw7 or -Cw8, which are recognized by p58 killer-cell 
      inhibitor receptor clone 43. We have determined the X-ray structure of the p58 
      NK-cell inhibitory receptor clone 42 at 1.7-A resolution. The structure has 
      tandem immunoglobulin-like domains positioned at an acute, 60-degree angle. Loops 
      on the outside of the elbow between the domains form a binding site projected 
      away from the NK-cell surface. The topology of the domains and their arrangement 
      relative to each other reveal a relationship to the haematopoietic receptor 
      family, with implications for the signalling mechanism in NK cells.
FAU - Fan, Q R
AU  - Fan QR
AD  - Department of Molecular and Cellular Biology, Howard Hughes Medical Institute, 
      Harvard University, Cambridge, Massachusetts 02138, USA. fan@crystal.harvard.edu
FAU - Mosyak, L
AU  - Mosyak L
FAU - Winter, C C
AU  - Winter CC
FAU - Wagtmann, N
AU  - Wagtmann N
FAU - Long, E O
AU  - Long EO
FAU - Wiley, D C
AU  - Wiley DC
LA  - eng
SI  - PDB/UNKNOWN
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (KIR2DL3 protein, human)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Receptors, KIR)
RN  - 0 (Receptors, KIR2DL3)
RN  - 0 (Recombinant Proteins)
SB  - IM
EIN - Nature 1997 Nov 20;390(6657):315
MH  - Binding Sites
MH  - Crystallography, X-Ray
MH  - Electrochemistry
MH  - Escherichia coli
MH  - Humans
MH  - Killer Cells, Natural/*chemistry/metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Receptors, Immunologic/*chemistry/metabolism
MH  - Receptors, KIR
MH  - Receptors, KIR2DL3
MH  - Recombinant Proteins/chemistry
MH  - Signal Transduction
EDAT- 1997/09/04 00:00
MHDA- 2001/03/23 10:01
CRDT- 1997/09/04 00:00
PHST- 1997/09/04 00:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1997/09/04 00:00 [entrez]
AID - 10.1038/38028 [doi]
PST - ppublish
SO  - Nature. 1997 Sep 4;389(6646):96-100. doi: 10.1038/38028.