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• 10.1109/icc.2011.5962704 Interference in wireless networks is one of the key
• JNC CR ICICS 2011 In this paper we propose a Joint Network Coding based
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Arq 5 0 1 Download Free Download

Structural Basis for CD96 Immune Receptor Recognition of Nectin-like Protein-5, CD155.

(2019) Structure 27: 219-228.e3

Arq 5 0 1 Download Free Windows 7

• PubMed: 30528596Search on PubMed
• DOI: 10.1016/j.str.2018.10.023
• Primary Citation of Related Structures:
  6ARQ


• PubMed Abstract:
  

CD96, DNAM-1, and TIGIT constitute a group of immunoglobulin superfamily receptors that are key regulators of tumor immune surveillance. Within this axis, CD96 recognizes the adhesion molecule nectin-like protein-5 (necl-5), although the molecular basis underpinning this interaction remains unclear ...

CD96, DNAM-1, and TIGIT constitute a group of immunoglobulin superfamily receptors that are key regulators of tumor immune surveillance. Within this axis, CD96 recognizes the adhesion molecule nectin-like protein-5 (necl-5), although the molecular basis underpinning this interaction remains unclear. We show that the first immunoglobulin domain (D1) of CD96 is sufficient to mediate a robust interaction with necl-5, but not the DNAM-1 and TIGIT ligand, nectin-2. The crystal structure of CD96-D1 bound to the necl-5 ectodomain revealed that CD96 recognized necl-5 D1 via a conserved 'lock-and-key' interaction observed across TIGIT:necl complexes. Specific necl-5 recognition was underpinned by a novel structural motif within CD96, namely an 'ancillary key'. Mutational analysis showed that this specific residue was critical for necl-5 binding, while simultaneously providing insights into the unique ligand specificity of CD96.

Organizational Affiliation:

Infection and Immunity Program and The Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia; Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Monash University, Clayton, VIC 3800, Australia. Electronic address: richard.berry@monash.edu.