Killer cell immunoglobulin-like receptor 3DL1-mediated recognition of human leukocyte antigen B

@article{Vivian2011KillerCI,
  title={Killer cell immunoglobulin-like receptor 3DL1-mediated recognition of human leukocyte antigen B},
  author={Julian P. Vivian and Renee C. Duncan and Richard Berry and Geraldine M. O’Connor and Hugh H Reid and Travis Beddoe and Stephanie Gras and Philippa M. Saunders and Maya A. Olshina and Jacqueline M. L. Widjaja and Christopher M. Harpur and Jie Lin and Sebastien M. Maloveste and David A. Price and Bernard A. P. Lafont and Daniel W McVicar and Craig S. Clements and Andrew G. Brooks and Jamie Rossjohn},
  journal={Nature},
  year={2011},
  volume={479},
  pages={401-405}
}
Members of the killer cell immunoglobulin-like receptor (KIR) family, a large group of polymorphic receptors expressed on natural killer (NK) cells, recognize particular peptide-laden human leukocyte antigen (pHLA) class I molecules and have a pivotal role in innate immune responses. Allelic variation and extensive polymorphism within the three-domain KIR family (KIR3D, domains D0–D1–D2) affects pHLA binding specificity and is linked to the control of viral replication and the treatment outcome… CONTINUE READING
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Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
Although the two - domain KIR ( KIR2D ) and KIR3DL1 docked similarly onto HLA - C and HLA - B respectively , the corresponding D1-mediated interactions differed markedly , thereby providing insight into the specificity of KIR3DL1 for discrete HLA - A and HLA - B allotypes .
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