Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3
Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3
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DOI：
10.1016/s1074-7613(01)00241-2
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发表时间：
2001-12-01
期刊：
影响因子：
32.4
通讯作者：
Sun, PD
中科院分区：
文献类型：
--
作者：
Radaev, S;Rostro, B;Sun, PD
wNKG2D 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 beta 2m 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 a 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.
