4g59

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'''Unreleased structure'''
 
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The entry 4g59 is ON HOLD
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==Crystal structure of the murine cytomegalovirus MHC-I homolog m152 with ligand RAE-1 gamma==
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<StructureSection load='4g59' size='340' side='right'caption='[[4g59]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4g59]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Murid_betaherpesvirus_1 Murid betaherpesvirus 1] 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=4G59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G59 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.44&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g59 OCA], [https://pdbe.org/4g59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g59 RCSB], [https://www.ebi.ac.uk/pdbsum/4g59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g59 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RAE1C_MOUSE RAE1C_MOUSE] Acts as a ligand for NKG2D.<ref>PMID:10894171</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Natural killer (NK) cells are activated by engagement of the NKG2D receptor with ligands on target cells stressed by infection or tumorigenesis. Several human and rodent cytomegalovirus (CMV) immunoevasins down-regulate surface expression of NKG2D ligands. The mouse CMV MHC class I (MHC-I)-like m152/gp40 glycoprotein down-regulates retinoic acid early inducible-1 (RAE1) NKG2D ligands as well as host MHC-I. Here we describe the crystal structure of an m152/RAE1gamma complex and confirm the intermolecular contacts by mutagenesis. m152 interacts in a pincer-like manner with two sites on the alpha1 and alpha2 helices of RAE1 reminiscent of the NKG2D interaction with RAE1. This structure of an MHC-I-like immunoevasin/MHC-I-like ligand complex explains the binding specificity of m152 for RAE1 and allows modeling of the interaction of m152 with classical MHC-I and of related viral immunoevasins.
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Authors: Wang, R, Natarajan, K, Margulies, D.H
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Structural basis of mouse cytomegalovirus m152/gp40 interaction with RAE1gamma reveals a paradigm for MHC/MHC interaction in immune evasion.,Wang R, Natarajan K, Revilleza MJ, Boyd LF, Zhi L, Zhao H, Robinson H, Margulies DH Proc Natl Acad Sci U S A. 2012 Nov 19. PMID:23169621<ref>PMID:23169621</ref>
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Description: Crystal structure of the murine cytomegalovirus MHC-I homolog m152 with ligand RAE-1 gamma
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4g59" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Murid betaherpesvirus 1]]
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[[Category: Mus musculus]]
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[[Category: Margulies DH]]
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[[Category: Natarajan K]]
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[[Category: Wang R]]

Current revision

Crystal structure of the murine cytomegalovirus MHC-I homolog m152 with ligand RAE-1 gamma

PDB ID 4g59

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