1mpu: Difference between revisions

Revision as of 14:57, 21 February 2008

Crystal Structure of the free human NKG2D immunoreceptor

OverviewOverview

Engagement of diverse protein ligands (MIC-A/B, ULBP, Rae-1, or H60) by NKG2D immunoreceptors mediates elimination of tumorigenic or virally infected cells by natural killer and T cells. Three previous NKG2D-ligand complex structures show the homodimeric receptor interacting with the monomeric ligands in similar 2:1 complexes, with an equivalent surface on each NKG2D monomer binding intimately to a total of six distinct ligand surfaces. Here, the crystal structure of free human NKG2D and in silico and in vitro alanine-scanning mutagenesis analyses of the complex interfaces indicate that NKG2D recognition degeneracy is not explained by a classical induced-fit mechanism. Rather, the divergent ligands appear to utilize different strategies to interact with structurally conserved elements of the consensus NKG2D binding site.

About this StructureAbout this Structure

1MPU is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Symmetry recognizing asymmetry: analysis of the interactions between the C-type lectin-like immunoreceptor NKG2D and MHC class I-like ligands., McFarland BJ, Kortemme T, Yu SF, Baker D, Strong RK, Structure. 2003 Apr;11(4):411-22. PMID:12679019

Page seeded by OCA on Thu Feb 21 13:57:48 2008

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OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-Engagement of diverse protein ligands (MIC-A/B, ULBP, Rae-1, or H60) by, NKG2D immunoreceptors mediates elimination of tumorigenic or virally, infected cells by natural killer and T cells. Three previous NKG2D-ligand, complex structures show the homodimeric receptor interacting with the, monomeric ligands in similar 2:1 complexes, with an equivalent surface on, each NKG2D monomer binding intimately to a total of six distinct ligand, surfaces. Here, the crystal structure of free human NKG2D and in silico, and in vitro alanine-scanning mutagenesis analyses of the complex, interfaces indicate that NKG2D recognition degeneracy is not explained by, a classical induced-fit mechanism. Rather, the divergent ligands appear to, utilize different strategies to interact with structurally conserved, elements of the consensus NKG2D binding site.
+Engagement of diverse protein ligands (MIC-A/B, ULBP, Rae-1, or H60) by NKG2D immunoreceptors mediates elimination of tumorigenic or virally infected cells by natural killer and T cells. Three previous NKG2D-ligand complex structures show the homodimeric receptor interacting with the monomeric ligands in similar 2:1 complexes, with an equivalent surface on each NKG2D monomer binding intimately to a total of six distinct ligand surfaces. Here, the crystal structure of free human NKG2D and in silico and in vitro alanine-scanning mutagenesis analyses of the complex interfaces indicate that NKG2D recognition degeneracy is not explained by a classical induced-fit mechanism. Rather, the divergent ligands appear to utilize different strategies to interact with structurally conserved elements of the consensus NKG2D binding site.
 ==About this Structure==
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 [[Category: Baker, D.]]
 [[Category: Kortemme, T.]]
-[[Category: McFarland, B.J.]]
+[[Category: McFarland, B J.]]
-[[Category: Strong, R.K.]]
+[[Category: Strong, R K.]]
 [[Category: PO4]]
 [[Category: c-type lectin-like domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:25:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:48 2008''