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1qo3
From Proteopedia
(New page: 200px<br /> <applet load="1qo3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qo3, resolution 2.30Å" /> '''COMPLEX BETWEEN NK ...) |
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| - | [[Image:1qo3.gif|left|200px]]<br /> | + | [[Image:1qo3.gif|left|200px]]<br /><applet load="1qo3" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1qo3" size=" | + | |
caption="1qo3, resolution 2.30Å" /> | caption="1qo3, resolution 2.30Å" /> | ||
'''COMPLEX BETWEEN NK CELL RECEPTOR LY49A AND ITS MHC CLASS I LIGAND H-2DD'''<br /> | '''COMPLEX BETWEEN NK CELL RECEPTOR LY49A AND ITS MHC CLASS I LIGAND H-2DD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Natural killer (NK) cell function is regulated by NK receptors that | + | Natural killer (NK) cell function is regulated by NK receptors that interact with MHC class I (MHC-I) molecules on target cells. The murine NK receptor Ly49A inhibits NK cell activity by interacting with H-2D(d) through its C-type-lectin-like NK receptor domain. Here we report the crystal structure of the complex between the Ly49A NK receptor domain and unglycosylated H-2D(d). The Ly49A dimer interacts extensively with two H-2D(d) molecules at distinct sites. At one interface, a single Ly49A subunit contacts one side of the MHC-I peptide-binding platform, presenting an open cavity towards the conserved glycosylation site on the H-2D(d) alpha2 domain. At a second, larger interface, the Ly49A dimer binds in a region overlapping the CD8-binding site. The smaller interface probably represents the interaction between Ly49A on the NK cell and MHC-I on the target cell, whereas the larger one suggests an interaction between Ly49A and MHC-I on the NK cell itself. Both Ly49A binding sites on MHC-I are spatially distinct from that of the T-cell receptor. |
==About this Structure== | ==About this Structure== | ||
| - | 1QO3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1QO3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Mariuzza, R | + | [[Category: Mariuzza, R A.]] |
[[Category: Tormo, J.]] | [[Category: Tormo, J.]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
| Line 27: | Line 26: | ||
[[Category: nk cell]] | [[Category: nk cell]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:53 2008'' |
Revision as of 12:41, 21 February 2008
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COMPLEX BETWEEN NK CELL RECEPTOR LY49A AND ITS MHC CLASS I LIGAND H-2DD
Overview
Natural killer (NK) cell function is regulated by NK receptors that interact with MHC class I (MHC-I) molecules on target cells. The murine NK receptor Ly49A inhibits NK cell activity by interacting with H-2D(d) through its C-type-lectin-like NK receptor domain. Here we report the crystal structure of the complex between the Ly49A NK receptor domain and unglycosylated H-2D(d). The Ly49A dimer interacts extensively with two H-2D(d) molecules at distinct sites. At one interface, a single Ly49A subunit contacts one side of the MHC-I peptide-binding platform, presenting an open cavity towards the conserved glycosylation site on the H-2D(d) alpha2 domain. At a second, larger interface, the Ly49A dimer binds in a region overlapping the CD8-binding site. The smaller interface probably represents the interaction between Ly49A on the NK cell and MHC-I on the target cell, whereas the larger one suggests an interaction between Ly49A and MHC-I on the NK cell itself. Both Ly49A binding sites on MHC-I are spatially distinct from that of the T-cell receptor.
About this Structure
1QO3 is a Protein complex structure of sequences from Human immunodeficiency virus and Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand., Tormo J, Natarajan K, Margulies DH, Mariuzza RA, Nature. 1999 Dec 9;402(6762):623-31. PMID:10604468
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