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