Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors

Nature ◽  
10.1038/38028 ◽  
1997 ◽  
Vol 389 (6646) ◽  
pp. 96-100 ◽  
Author(s):  
Qing R. Fan ◽  
Lidia Mosyak ◽  
Christine C. Winter ◽  
Nicolai Wagtmann ◽  
Eric O. Long ◽  
...  
PLoS ONE ◽  
2010 ◽  
Vol 5 (11) ◽  
pp. e15374 ◽  
Author(s):  
Karsten Köhler ◽  
Shiqiu Xiong ◽  
Joanna Brzostek ◽  
Maryam Mehrabi ◽  
Philipp Eissmann ◽  
...  

1999 ◽  
Vol 190 (6) ◽  
pp. 793-802 ◽  
Author(s):  
Michela Falco ◽  
Roberto Biassoni ◽  
Cristina Bottino ◽  
Massimo Vitale ◽  
Simona Sivori ◽  
...  

In this study, by the generation of a specific monoclonal antibody, we identified p75/AIRM1 (for adhesion inhibitory receptor molecule 1), a novel inhibitory receptor that is mostly confined to human natural killer cells. p75/AIRM1 is a 75-kD glycoprotein that, upon sodium pervanadate treatment, becomes tyrosine phosphorylated and associates to src homology 2 domain–bearing protein tyrosine phosphatase (SHP)-1. The p75/AIRM1 gene is located on human chromosome 19 and encodes a novel member of the sialoadhesin family characterized by three immunoglobulin-like extracellular domains (one NH2-terminal V-type and two C2-type) and a classical immunoreceptor tyrosine–based inhibitory motif (ITIM) in the cytoplasmic portion. The highest amino acid sequence similarity has been found with the myeloid-specific CD33 molecule and the placental CD33L1 protein. Similar to other sialoadhesin molecules, p75/AIRM1 appears to mediate sialic acid–dependent ligand recognition.


Nature ◽  
10.1038/36911 ◽  
1997 ◽  
Vol 390 (6657) ◽  
pp. 315-315 ◽  
Author(s):  
Qing R. Fan ◽  
Lidia Mosyak ◽  
Christine C. Winter ◽  
Nicolai Wagtmann ◽  
Eric O. Long ◽  
...  

iScience ◽  
2019 ◽  
Vol 11 ◽  
pp. 466-473 ◽  
Author(s):  
Natan Stein ◽  
Orit Berhani ◽  
Dominik Schmiedel ◽  
Alexandra Duev-Cohen ◽  
Einat Seidel ◽  
...  

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