1HKF

The three dimensional structure of NK cell receptor Nkp44, a triggering partner in natural cytotoxicity

Summary for 1HKF

• Entry DOI: 10.2210/pdb1hkf/pdb
• Descriptor: NK CELL ACTIVATING RECEPTOR (2 entities in total)
• Functional Keywords: natural cytotoxicity receptor, nkp44, receptor, immunoglobulin domain
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cell membrane; Single-pass type I membrane protein (Potential): O95944
• Total number of polymer chains: 1
• Total formula weight: 13957.73

Authors

Ponassi, M.,Cantoni, C.,Biassoni, R.,Conte, R.,Spallarossa, A.,Moretta, A.,Moretta, L.,Bolognesi, M.,Bordo, D. (deposition date: 2003-03-10, release date: 2003-06-11, Last modification date: 2024-10-23)

Primary citation

Cantoni, C.,Ponassi, M.,Biassoni, R.,Conte, R.,Spallarossa, A.,Moretta, A.,Moretta, L.,Bolognesi, M.,Bordo, D.
The Three-Dimensional Structure of the Human Nk Cell Receptor Nkp44, a Triggering Partner in Natural Cytotoxicity
Structure, 11:725-, 2003

PubMed 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.

PubMed: 12791260
DOI: 10.1016/S0969-2126(03)00095-9

Experimental method

X-RAY DIFFRACTION (2.2 Å)