TABLE 2.

Corroboration between experimental data and our computational model of E1/E2

Criterion and residue(s)	Protein	Correspondence with expt	Experimental method	Reference(s)
Criteria used as constraints during modeling
192–270	E1	Homology model based on structures reported under PDB accession no. 4UOI and 1LN2	Crystallography	20, 34
421–645	E2	Same as structure reported under PDB accession no. 4MWF	Crystallography	19
C652, C677	E2	Disulfide bonded	Ab binding patterns upon mutation	32
352–378, 716–738	E1/E2	Single-domain helices	NMR; fluorescent imaging of epitope-tagged C termini	28, 29
K370, D728	E1/E2	Salt bridge between TMDs of E1 and E2	Mutational analysis	29, 54–56
Criteria used to guide de novo model selection
201–206, 639, 657–659, 692, 698	E1/E2	Residues are proximal to each other	Required for binding to E1/E2 by AR4A and/or AR5A Abs	18
315–324, 333–338, 693–701, 713–717	E1/E2	Two α-helices exist in each of E1 and E2 stem domains	NMR studies of peptides	38, 50
Agreement with expt observed after modeling
192–238	E1	Near E1/E2 interface	Peptide binds to E2	35
271–304	E1	Extension of structural homology of E1 to structure reported under PDB accession no. 1LN2	Crystallography	34
H352	E1	Important for heterodimerization	Mutational analysis	58
480–487, 574–579	E2	HVR2 (residues 461–481), residues 484–491, and IgVR (residues 570–580) are essential for heterodimerization	Studies of deletion constructs	35, 59
541–548	E2	Near E1/E2 interface	Mutations of residues 523–545 affect binding to E1/E2 by E1-specific Ab A7	18
587, 651–703	E2	5-residue insertions at residue 587 or 692 affect heterodimerization	Linker-scanning mutagenesis	60
L675, S678, H691	E2	L675, S678, and H691 are all determinants of heterodimerization	Mutational analysis	57