1kcg: Difference between revisions

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[[Image:1kcg.gif|left|200px]]
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{{STRUCTURE_1kcg|  PDB=1kcg  |  SCENE=  }}  
{{STRUCTURE_1kcg|  PDB=1kcg  |  SCENE=  }}  


'''NKG2D in complex with ULBP3'''
===NKG2D in complex with ULBP3===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11754823}}


==About this Structure==
==About this Structure==
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[[Category: Mhc class i-like molecule]]
[[Category: Mhc class i-like molecule]]
[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
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Revision as of 07:07, 2 July 2008

File:1kcg.png

Template:STRUCTURE 1kcg

NKG2D in complex with ULBP3

Template:ABSTRACT PUBMED 11754823

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

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