1p4l: Difference between revisions

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[[Image:1p4l.gif|left|200px]]<br /><applet load="1p4l" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1p4l.gif|left|200px]]<br /><applet load="1p4l" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1p4l, resolution 2.90Å" />

'''Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb'''<br />

==Overview==

The Ly49 family of natural killer (NK) receptors regulates NK cell, function by sensing major histocompatibility complex (MHC) class I. Ly49, receptors show complex patterns of MHC class I cross-reactivity and, in, certain cases, peptide selectivity. To investigate whether specificity, differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in, complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules, in symmetrical way, a mode distinct from that of Ly49A, which binds MHC, class I asymmetrically. Ly49C does not directly contact the MHC-bound, peptide. In addition, MHC crosslinking by Ly49C was demonstrated in, solution. We propose a dynamic model for Ly49-MHC class I interactions, involving conformational changes in the receptor, whereby variations in, Ly49 dimerization mediate different MHC-binding modes.

The Ly49 family of natural killer (NK) receptors regulates NK cell function by sensing major histocompatibility complex (MHC) class I. Ly49 receptors show complex patterns of MHC class I cross-reactivity and, in certain cases, peptide selectivity. To investigate whether specificity differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules in symmetrical way, a mode distinct from that of Ly49A, which binds MHC class I asymmetrically. Ly49C does not directly contact the MHC-bound peptide. In addition, MHC crosslinking by Ly49C was demonstrated in solution. We propose a dynamic model for Ly49-MHC class I interactions involving conformational changes in the receptor, whereby variations in Ly49 dimerization mediate different MHC-binding modes.

==About this Structure==

1P4L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1P4L OCA].

1P4L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4L OCA].

==Reference==

Line 16:

[[Category: Dimasi, N.]]

[[Category: Guan, R.]]

[[Category: Mariuzza, R.A.]]

[[Category: Mariuzza, R A.]]

[[Category: Natarajan, K.]]

[[Category: c-type lectin-like domain]]

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[[Category: natural killer receptor]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:02 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1p4l.gif|left|200px]]<br /><applet load="1p4l" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1p4l.gif|left|200px]]<br /><applet load="1p4l" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1p4l, resolution 2.90&Aring;" />
 '''Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb'''<br />
 ==Overview==
-The Ly49 family of natural killer (NK) receptors regulates NK cell, function by sensing major histocompatibility complex (MHC) class I. Ly49, receptors show complex patterns of MHC class I cross-reactivity and, in, certain cases, peptide selectivity. To investigate whether specificity, differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in, complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules, in symmetrical way, a mode distinct from that of Ly49A, which binds MHC, class I asymmetrically. Ly49C does not directly contact the MHC-bound, peptide. In addition, MHC crosslinking by Ly49C was demonstrated in, solution. We propose a dynamic model for Ly49-MHC class I interactions, involving conformational changes in the receptor, whereby variations in, Ly49 dimerization mediate different MHC-binding modes.
+The Ly49 family of natural killer (NK) receptors regulates NK cell function by sensing major histocompatibility complex (MHC) class I. Ly49 receptors show complex patterns of MHC class I cross-reactivity and, in certain cases, peptide selectivity. To investigate whether specificity differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules in symmetrical way, a mode distinct from that of Ly49A, which binds MHC class I asymmetrically. Ly49C does not directly contact the MHC-bound peptide. In addition, MHC crosslinking by Ly49C was demonstrated in solution. We propose a dynamic model for Ly49-MHC class I interactions involving conformational changes in the receptor, whereby variations in Ly49 dimerization mediate different MHC-binding modes.
 ==About this Structure==
-P4L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P4L OCA].
+P4L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4L OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Dimasi, N.]]
 [[Category: Guan, R.]]
-[[Category: Mariuzza, R.A.]]
+[[Category: Mariuzza, R A.]]
 [[Category: Natarajan, K.]]
 [[Category: c-type lectin-like domain]]
@@ Line 23: / Line 23: @@
 [[Category: natural killer receptor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:28:20 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:02 2008''