4pn6: Difference between revisions
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The | ==Structure of the Cytomegalovirus-Encoded m04 Glycoprotein== | ||
<StructureSection load='4pn6' size='340' side='right'caption='[[4pn6]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4pn6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Muromegalovirus_G4 Muromegalovirus G4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PN6 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]] 3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4pn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pn6 OCA], [https://pdbe.org/4pn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pn6 RCSB], [https://www.ebi.ac.uk/pdbsum/4pn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pn6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B3UWV7_MUHV1 B3UWV7_MUHV1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ability of cytomegaloviruses (CMV) to evade the host's immune system is dependent on the expression of a wide array of glycoproteins, many of which interfere with natural killer (NK) cell function. In murine CMV, two large protein families mediate this immune-evasive function. While it is established that the m145 family members mimic the structure of major histocompatibility complex (MHC)-I molecules, the structure of the m02 family remains unknown. The most extensively studied m02 family member is m04, a glycoprotein that escorts newly assembled MHC-I molecules to the cell surface, presumably to avoid missing-self recognition. Here we report the crystal structure of the m04 ectodomain, thereby providing insight into this large immunoevasin family. m04 adopted a beta-sandwich immunoglobulin variable (Ig-V) like fold, despite sharing very little sequence identity with the Ig-V superfamily. In addition to the Ig-V core, m04 possesses several unique structural features that included an unusual beta-strand topology, a number of extended loops and a prominent alpha-helix. The m04 interior was packed by a myriad of hydrophobic residues that form distinct clusters around two conserved tryptophan residues. This hydrophobic core was well conserved throughout the m02 family, thereby indicating that MCMV encodes a number of Ig-V like molecules. We show that m04 binds a range of MHC-I molecules with low affinity in a peptide-independent manner. Accordingly the structure of m04, which represents the first example of an MCMV encoded Ig-V fold, provides a basis for understanding the structure and function of this enigmatic and large family of immunoevasins. | |||
The Structure of the Cytomegalovirus-Encoded m04 Glycoprotein, a Prototypical Member of the m02 Family of Immunoevasins.,Berry R, Vivian JP, Deuss FA, Balaji GR, Saunders PM, Lin J, Littler DR, Brooks AG, Rossjohn J J Biol Chem. 2014 Jun 30. pii: jbc.M114.584128. PMID:24982419<ref>PMID:24982419</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4pn6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Muromegalovirus G4]] | |||
[[Category: Berry R]] | |||
[[Category: Rossjohn J]] |