1kcg: Difference between revisions
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'''NKG2D in complex with ULBP3''' | '''NKG2D in complex with ULBP3''' | ||
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[[Category: Radaev, S.]] | [[Category: Radaev, S.]] | ||
[[Category: Sun, P.]] | [[Category: Sun, P.]] | ||
[[Category: | [[Category: C-type lectin-like receptor]] | ||
[[Category: | [[Category: Mhc class i-like molecule]] | ||
[[Category: | [[Category: Protein-protein complex]] | ||
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Revision as of 19:34, 2 May 2008
NKG2D in complex with ULBP3
Overview
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.
About this Structure
1KCG is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3., Radaev S, Rostro B, Brooks AG, Colonna M, Sun PD, Immunity. 2001 Dec;15(6):1039-49. PMID:11754823 Page seeded by OCA on Fri May 2 22:34:23 2008
