1m4k: Difference between revisions

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==Overview==

Killer cell Ig-like receptors (KIRs) regulate the function of human, natural killer and T cell subsets. A feature of the KIR locus is the, clustering of homologous genes encoding for inhibitory and activating KIR., Inhibitory and activating KIR differ for ligand specificities and/or, affinities. In particular, we show here with KIR tetramers that activating, KIR2DS2 does not bind HLA-Cw3 molecules recognized by inhibitory KIR2DL2, despite 99% extracellular amino acid identity. We also report the 2.3-A, structure of KIR2DS2, which reveals subtle displacements of two residues, (Tyr45 and Gln71) involved in the interaction of KIR2DL2 with HLA-Cw3., These results show that KIR molecules cannot tolerate any variability in, their three-dimensional structure without altering their MHC class I, recognition capacities. Therefore, the mode of recognition used by KIR, largely differs from the conformational changes that characterize T cell, receptor or NKG2D interaction with their respective ligands.

Killer cell Ig-like receptors (KIRs) regulate the function of human natural killer and T cell subsets. A feature of the KIR locus is the clustering of homologous genes encoding for inhibitory and activating KIR. Inhibitory and activating KIR differ for ligand specificities and/or affinities. In particular, we show here with KIR tetramers that activating KIR2DS2 does not bind HLA-Cw3 molecules recognized by inhibitory KIR2DL2, despite 99% extracellular amino acid identity. We also report the 2.3-A structure of KIR2DS2, which reveals subtle displacements of two residues (Tyr45 and Gln71) involved in the interaction of KIR2DL2 with HLA-Cw3. These results show that KIR molecules cannot tolerate any variability in their three-dimensional structure without altering their MHC class I recognition capacities. Therefore, the mode of recognition used by KIR largely differs from the conformational changes that characterize T cell receptor or NKG2D interaction with their respective ligands.

==About this Structure==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Gastinel, L.N.]]

[[Category: Gastinel, L N.]]

[[Category: Saulquin, X.]]

[[Category: Vivier, E.]]

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[[Category: ig-like c2 type domain]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:21 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Killer cell Ig-like receptors (KIRs) regulate the function of human, natural killer and T cell subsets. A feature of the KIR locus is the, clustering of homologous genes encoding for inhibitory and activating KIR., Inhibitory and activating KIR differ for ligand specificities and/or, affinities. In particular, we show here with KIR tetramers that activating, KIR2DS2 does not bind HLA-Cw3 molecules recognized by inhibitory KIR2DL2, despite 99% extracellular amino acid identity. We also report the 2.3-A, structure of KIR2DS2, which reveals subtle displacements of two residues, (Tyr45 and Gln71) involved in the interaction of KIR2DL2 with HLA-Cw3., These results show that KIR molecules cannot tolerate any variability in, their three-dimensional structure without altering their MHC class I, recognition capacities. Therefore, the mode of recognition used by KIR, largely differs from the conformational changes that characterize T cell, receptor or NKG2D interaction with their respective ligands.
+Killer cell Ig-like receptors (KIRs) regulate the function of human natural killer and T cell subsets. A feature of the KIR locus is the clustering of homologous genes encoding for inhibitory and activating KIR. Inhibitory and activating KIR differ for ligand specificities and/or affinities. In particular, we show here with KIR tetramers that activating KIR2DS2 does not bind HLA-Cw3 molecules recognized by inhibitory KIR2DL2, despite 99% extracellular amino acid identity. We also report the 2.3-A structure of KIR2DS2, which reveals subtle displacements of two residues (Tyr45 and Gln71) involved in the interaction of KIR2DL2 with HLA-Cw3. These results show that KIR molecules cannot tolerate any variability in their three-dimensional structure without altering their MHC class I recognition capacities. Therefore, the mode of recognition used by KIR largely differs from the conformational changes that characterize T cell receptor or NKG2D interaction with their respective ligands.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Gastinel, L.N.]]
+[[Category: Gastinel, L N.]]
 [[Category: Saulquin, X.]]
 [[Category: Vivier, E.]]
@@ Line 21: / Line 21: @@
 [[Category: ig-like c2 type domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:21:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:21 2008''