1p4l
From Proteopedia
(New page: 200px<br /><applet load="1p4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p4l, resolution 2.90Å" /> '''Crystal structure of...) |
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| - | [[Image:1p4l.gif|left|200px]]<br /><applet load="1p4l" size=" | + | [[Image:1p4l.gif|left|200px]]<br /><applet load="1p4l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p4l, resolution 2.90Å" /> | caption="1p4l, resolution 2.90Å" /> | ||
'''Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb'''<br /> | '''Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Ly49 family of natural killer (NK) receptors regulates NK cell | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Dimasi, N.]] | [[Category: Dimasi, N.]] | ||
[[Category: Guan, R.]] | [[Category: Guan, R.]] | ||
| - | [[Category: Mariuzza, R | + | [[Category: Mariuzza, R A.]] |
[[Category: Natarajan, K.]] | [[Category: Natarajan, K.]] | ||
[[Category: c-type lectin-like domain]] | [[Category: c-type lectin-like domain]] | ||
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[[Category: natural killer receptor]] | [[Category: natural killer receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:02 2008'' |
Revision as of 12:25, 21 February 2008
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Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb
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.
About this Structure
1P4L is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b)., Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA, Nat Immunol. 2003 Dec;4(12):1213-22. Epub 2003 Nov 2. PMID:14595439
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