1mpu: Difference between revisions

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==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''

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@@ 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==
@@ Line 15: / Line 15: @@
 [[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''