1KCG

NKG2D in complex with ULBP3

Summary for 1KCG

• Entry DOI: 10.2210/pdb1kcg/pdb
• Descriptor: NKG2-D type II integral membrane protein, UL16-binding protein 3 (3 entities in total)
• Functional Keywords: protein-protein complex, c-type lectin-like receptor, mhc class i-like molecule, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type II membrane protein: P26718; Cell membrane; Lipid-anchor, GPI-anchor: Q9BZM4
• Total number of polymer chains: 3
• Total formula weight: 50160.87

Authors

Radaev, S.,Sun, P. (deposition date: 2001-11-08, release date: 2002-01-09, Last modification date: 2024-12-25)

Primary citation

Radaev, S.,Rostro, B.,Brooks, A.G.,Colonna, M.,Sun, P.D.
Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3.
Immunity, 15:1039-1049, 2001

PubMed Abstract: NKG2D is known to trigger the natural killer (NK) cell lysis of various tumor and virally infected cells. In the NKG2D/ULBP3 complex, the structure of ULBP3 resembles the alpha1 and alpha2 domains of classical MHC molecules without a bound peptide. The lack of alpha3 and beta2m domains is compensated by replacing two hydrophobic patches at the underside of the class I MHC-like beta sheet floor with a group of hydrophilic and charged residues in ULBP3. NKG2D binds diagonally across the ULBP3 alpha helices, creating a complementary interface, an asymmetrical subunit orientation, and local conformational adjustments in the receptor. The interface is stabilized primarily by hydrogen bonds and hydrophobic interactions. Unlike the KIR receptors that recognize a conserved HLA region by a lock-and-key mechanism, NKG2D recognizes diverse ligands by an induced-fit mechanism.

PubMed: 11754823
DOI: 10.1016/S1074-7613(01)00241-2

Experimental method

X-RAY DIFFRACTION (2.6 Å)