The three-dimensional structure of the human NK cell receptor NKp44, a triggering partner in natural cytotoxicity
The three-dimensional structure of the human NK cell receptor NKp44, a triggering partner in natural cytotoxicity
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DOI:
10.1016/s0969-2126(03)00095-9
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发表时间:
2003-06-01
期刊:
影响因子:
5.7
通讯作者:
Bordo, D
中科院分区:
文献类型:
--
作者:
Cantoni, C;Ponassi, M;Bordo, D
Natural killer (NK) cells direct cytotoxicity against tumor or virally infected cells. NK cell activation depends on a fine balance between inhibitory and activating receptors. NKp44 is a cytotoxicity activating receptor composed of one Ig-like extracellular domain, a transmembrane segment, and a cytoplasmic domain. The 2.2 Angstrom crystal structure shows that the NKp44 Ig domain forms a saddle-shaped dimer, where a charged surface groove protrudes from the core structure in each subunit. NKp44 Ig domain disulfide bridge topology defines a new Ig structural subfamily. The data presented are a first step toward understanding the molecular basis for ligand recognition by natural cytotoxicity receptors, whose key role in the immune system is established, but whose cellular ligands are still elusive.