View source for 7lyw


==Crystal structure of the HCMV pentamer-specific antibody 2-25==
<StructureSection load='7lyw' size='340' side='right'caption='[[7lyw]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7lyw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LYW 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]] 2.51&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=7lyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lyw OCA], [https://pdbe.org/7lyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lyw RCSB], [https://www.ebi.ac.uk/pdbsum/7lyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lyw ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human cytomegalovirus (HCMV) encodes multiple surface glycoprotein complexes to infect a variety of cell types. The HCMV Pentamer, composed of gH, gL, UL128, UL130, and UL131A, enhances entry into epithelial, endothelial, and myeloid cells by interacting with the cell surface receptor neuropilin 2 (NRP2). Despite the critical nature of this interaction, the molecular determinants that govern NRP2 recognition remain unclear. Here, we describe the cryo-EM structure of NRP2 bound to Pentamer. The high-affinity interaction between these proteins is calcium dependent and differs from the canonical carboxyl-terminal arginine (CendR) binding that NRP2 typically uses. We also determine the structures of four neutralizing human antibodies bound to the HCMV Pentamer to define susceptible epitopes. Two of these antibodies compete with NRP2 binding, but the two most potent antibodies recognize a previously unidentified epitope that does not overlap the NRP2-binding site. Collectively, these findings provide a structural basis for HCMV tropism and antibody-mediated neutralization.

Structural basis for HCMV Pentamer recognition by neuropilin 2 and neutralizing antibodies.,Wrapp D, Ye X, Ku Z, Su H, Jones HG, Wang N, Mishra AK, Freed DC, Li F, Tang A, Li L, Jaijyan DK, Zhu H, Wang D, Fu TM, Zhang N, An Z, McLellan JS Sci Adv. 2022 Mar 11;8(10):eabm2546. doi: 10.1126/sciadv.abm2546. Epub 2022 Mar , 11. PMID:35275718<ref>PMID:35275718</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lyw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: McLellan JS]]
[[Category: Mishra AK]]
[[Category: Wrapp D]]