1qo3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1qo3.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1qo3", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1qo3|  PDB=1qo3  |  SCENE=  }}
'''COMPLEX BETWEEN NK CELL RECEPTOR LY49A AND ITS MHC CLASS I LIGAND H-2DD'''


==Complex between NK cell receptor Ly49A and its MHC class I ligand H-2Dd==
<StructureSection load='1qo3' size='340' side='right'caption='[[1qo3]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qo3]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QO3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo3 OCA], [https://pdbe.org/1qo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qo3 RCSB], [https://www.ebi.ac.uk/pdbsum/1qo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qo3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA12_MOUSE HA12_MOUSE] Involved in the presentation of foreign antigens to the immune system.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/1qo3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qo3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:10604468</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1QO3 is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO3 OCA].
</div>
<div class="pdbe-citations 1qo3" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10604468 10604468]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[MHC 3D structures|MHC 3D structures]]
*[[MHC I 3D structures|MHC I 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human immunodeficiency virus]]
[[Category: Human immunodeficiency virus]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Mariuzza RA]]
[[Category: Mariuzza, R A.]]
[[Category: Tormo J]]
[[Category: Tormo, J.]]
[[Category: B2m]]
[[Category: C-type lectin-like]]
[[Category: Histocompatibility]]
[[Category: Inhibitory receptor]]
[[Category: Ly-49]]
[[Category: Ly49]]
[[Category: Mhc-i]]
[[Category: Nk cell]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:30:26 2008''

Latest revision as of 12:50, 13 December 2023

Complex between NK cell receptor Ly49A and its MHC class I ligand H-2Dd

1qo3, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1qo3&oldid=3982276"