1ydp: Difference between revisions

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[[Image:1ydp.gif|left|200px]]


{{Structure
==1.9A crystal structure of HLA-G==
|PDB= 1ydp |SIZE=350|CAPTION= <scene name='initialview01'>1ydp</scene>, resolution 1.9&Aring;
<StructureSection load='1ydp' size='340' side='right'caption='[[1ydp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>
<table><tr><td colspan='2'>[[1ydp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YDP FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ydp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ydp OCA], [https://pdbe.org/1ydp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ydp RCSB], [https://www.ebi.ac.uk/pdbsum/1ydp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ydp ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ydp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ydp OCA], [http://www.ebi.ac.uk/pdbsum/1ydp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ydp RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/HLAG_HUMAN HLAG_HUMAN] Involved in the presentation of foreign antigens to the immune system. Plays a role in maternal tolerance of the fetus by mediating protection from the deleterious effects of natural killer cells, cytotoxic T-lymphocytes, macrophages and mononuclear cells.
== 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/yd/1ydp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ydp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
HLA-G is a nonclassical major histocompatibility complex class I (MHC-I) molecule that is primarily expressed at the fetal-maternal interface, where it is thought to play a role in protecting the fetus from the maternal immune response. HLA-G binds a limited repertoire of peptides and interacts with the inhibitory leukocyte Ig-like receptors LIR-1 and LIR-2 and possibly with certain natural killer cell receptors. To gain further insights into HLA-G function, we determined the 1.9-A structure of a monomeric HLA-G complexed to a natural endogenous peptide ligand from histone H2A (RIIPRHLQL). An extensive network of contacts between the peptide and the antigen-binding cleft reveal a constrained mode of binding reminiscent of the nonclassical HLA-E molecule, thereby providing a structural basis for the limited peptide repertoire of HLA-G. The alpha3 domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory receptors, is structurally distinct from the alpha3 domains of classical MHC-I molecules, providing a rationale for the observed affinity differences for these ligands. The structural data suggest a head-to-tail mode of dimerization, mediated by an intermolecular disulfide bond, that is consistent with the observation of HLA-G dimers on the cell surface.


'''1.9A crystal structure of HLA-G'''
Crystal structure of HLA-G: a nonclassical MHC class I molecule expressed at the fetal-maternal interface.,Clements CS, Kjer-Nielsen L, Kostenko L, Hoare HL, Dunstone MA, Moses E, Freed K, Brooks AG, Rossjohn J, McCluskey J Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3360-5. Epub 2005 Feb 17. PMID:15718280<ref>PMID:15718280</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ydp" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
HLA-G is a nonclassical major histocompatibility complex class I (MHC-I) molecule that is primarily expressed at the fetal-maternal interface, where it is thought to play a role in protecting the fetus from the maternal immune response. HLA-G binds a limited repertoire of peptides and interacts with the inhibitory leukocyte Ig-like receptors LIR-1 and LIR-2 and possibly with certain natural killer cell receptors. To gain further insights into HLA-G function, we determined the 1.9-A structure of a monomeric HLA-G complexed to a natural endogenous peptide ligand from histone H2A (RIIPRHLQL). An extensive network of contacts between the peptide and the antigen-binding cleft reveal a constrained mode of binding reminiscent of the nonclassical HLA-E molecule, thereby providing a structural basis for the limited peptide repertoire of HLA-G. The alpha3 domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory receptors, is structurally distinct from the alpha3 domains of classical MHC-I molecules, providing a rationale for the observed affinity differences for these ligands. The structural data suggest a head-to-tail mode of dimerization, mediated by an intermolecular disulfide bond, that is consistent with the observation of HLA-G dimers on the cell surface.
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
 
*[[MHC 3D structures|MHC 3D structures]]
==About this Structure==
*[[MHC I 3D structures|MHC I 3D structures]]
1YDP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YDP OCA].
== References ==
 
<references/>
==Reference==
__TOC__
Crystal structure of HLA-G: a nonclassical MHC class I molecule expressed at the fetal-maternal interface., Clements CS, Kjer-Nielsen L, Kostenko L, Hoare HL, Dunstone MA, Moses E, Freed K, Brooks AG, Rossjohn J, McCluskey J, Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3360-5. Epub 2005 Feb 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15718280 15718280]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Brooks, A G.]]
[[Category: Synthetic construct]]
[[Category: Clements, C S.]]
[[Category: Brooks AG]]
[[Category: Dunstone, M A.]]
[[Category: Clements CS]]
[[Category: Freed, K.]]
[[Category: Dunstone MA]]
[[Category: Hoare, H L.]]
[[Category: Freed K]]
[[Category: Kjer-nielsen, L.]]
[[Category: Hoare HL]]
[[Category: Kostenko, L.]]
[[Category: Kjer-nielsen L]]
[[Category: Mccluskey, J.]]
[[Category: Kostenko L]]
[[Category: Moses, E.]]
[[Category: Mccluskey J]]
[[Category: Rossjohn, J.]]
[[Category: Moses E]]
[[Category: immune system]]
[[Category: Rossjohn J]]
 
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