The E-L-E-F-N motif is located in a putative beta-hairpin at the KSHV and RRV gH/gL interaction site. Anna K. Großkopf Armin Ensser Frank Neipel Doris Jungnickl Sarah Schlagowski Ronald C. Desrosiers Alexander S. Hahn 10.1371/journal.ppat.1006912.g003 https://plos.figshare.com/articles/figure/The_E-L-E-F-N_motif_is_located_in_a_putative_beta-hairpin_at_the_KSHV_and_RRV_gH_gL_interaction_site_/5880802 <p>Homology-based structure prediction of the KSHV gH/gL and RRV gH/gL complexes based on the crystal structure of the EBV gH/gL complex (PDB number 3PHF) using the Iterative Threading ASSembly Refinement (I-TASSER) server and the CO-THreader algorithms for protein-protein complex structure and multi-chain protein threading. <b>A</b> KSHV gH/gL complex. Domain I is colored in blue. gL is colored in green. <b>B</b> Enlarged view of the inset indicated in A by dotted lines, showing the E-L-E-F-N motif in a putative beta-hairpin. Amino acids Glu52 and Phe53 that are critical for Eph binding are highlighted by asterisks. <b>C</b> RRV gH/gL complex. Domain I is colored in blue. gL is colored in green. <b>D</b> Enlarged view of the inset indicated in C by dotted lines, showing the E-L-E-F-N motif in a putative beta-hairpin. Amino acids Glu54 and Phe55 that are critical for Eph binding are highlighted by asterisks.</p> 2018-02-12 18:46:56 Eph family receptor tyrosine kinases KSHV strains gH protein-protein interactions oncogenic virus Eph-binding residues Eph-binding-negative RRV mutants rhesus monkey rhadinovirus nonhuman primates N-terminal domain sequence analysis RRV glycoprotein H B-cell malignancies log order RRV gL Eph family receptor-binding motif entry mediators Inhibition experiments cell types host factors gL expression cell type-specific use Eph-interaction motif