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The three-dimensional structure of the human NK cell receptor NKp44, a triggering partner in natural cytotoxicity.

Cantoni C, Ponassi M, Biassoni R, Conte R, Spallarossa A, Moretta A, Moretta L, Bolognesi M, Bordo D
Structure 11 725-34 (2003)
Cited: 70 times
EuropePMC logo PMID: 12791260

Abstract

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 A 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.

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Articles citing this publication (49)

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