Table 1.
Experimentally determined structures of E1, E2, and monoclonal antibodies.
| Structure codea | Hepatitis C virus (HCV) glycoproteinb | Residue rangec | Antibody | Reference |
|---|---|---|---|---|
| X-ray crystallography | ||||
| 4UOI | E1 | 192–270 | – | (38) |
| 4N0Y | E1 | 314–324 | IGH526 | (39) |
| 4GAG | E2 | 411–424 | AP33 | (40) |
| 4GAJ | E2 | 412–423 | AP33 | (40) |
| 4GAY | E2 | Unbound mAb | AP33 | (40) |
| 4DGY, 4DGV | E2 | 412–423 | HCV1 | (41) |
| 4G6A | E2 | 412–423 | AP33 | (42) |
| 4HS6 | E2 | 412–423 | MRCT10.362 | (43) |
| 4HS8 | E2 | 412–423 | hu5B3.v3 | (43) |
| 4WHT, 4WHY | E2 | 412–423 | 3/11 | (35) |
| 4XVJ | E2 | 412–423 | HC33.1 | (44) |
| 5FGB | E2 | 417–421 | HC33.4 | (45) |
| 5FGC | E2 | 415–423 | HC33.8 | (45) |
| 5EOC | E2 | 412–422d | C2 | (16) |
| 5KZP | E2 | 412–423d | HCV1 | (17) |
| 5VXR | E2 | 412–423 | MAb24 | (46) |
| 4MWF | E2 | 421–645e | AR3C | (47) |
| 4WEB | E2 | 486–645 | 2A12 | (48) |
| 4Q0X | E2 | 434–442 | mAb#12 | (49) |
| 4HZL | E2 | 430–442 | mAb#8 | (50) |
| 4JZN | E2 | 435–446 | HC84.1 | (51) |
| 4JZO | E2 | 436–446 | HC84.27 | (51) |
| 5ERW | E2 | 438–446 | HC84.26 | –f |
| 5ESA | E2 | Unbound mAb | HC84.26 | –f |
| 4Z0X | E2 | 435–446 | HC84.26.5D | (52) |
| 5NPH, 5NPI, 5NPJ | E2 | 532–540 | DAO5 | (53) |
| 3U6R | E2 | Unbound mAb | 1:7 | (54) |
| 4JVP | E2 | Unbound nanobody | D03 | (55) |
| Nuclear magnetic resonance | ||||
| 1EMZ | E1 | 350–370 | – | (56) |
| 2KNU | E1 | 314–342 | – | (57) |
| 2KZQ | E2 | 684–719 | – | (58) |
| Electron microscopyg | ||||
| 5759 | E2 | 384–717 | AR3A | (47) |
| 5760 | E2 | 384–717 | AR3A, AR2A | (47) |
| 5761 | E2 | 384–717 | AR2A, CD81 | (47) |
| 8338, 8339, 8340 | E2 | 412–645 | AR1B, AR2A, HCV1 | (36) |
aProtein Data Bank (59) or EMDataBank (60) codes shown. Multiple codes are shown in cases with multiple entries reported from same study containing the same residue range and binding partner(s), corresponding to different crystallographic symmetry forms, electron microscopy reconstructions, or HCV isolate sequences.
bIn the case of unbound antibody, glycoprotein target of antibody is given for reference.
cResidue numbering based on H77 isolate. For crystallographic structures, range reflects resolved residues present in coordinates.
dCyclic epitope-based designs are present in these structures.
eThis E2 core construct included engineered deletions of residues.
fThe coordinates for these X-ray structures have been released in the PDB (59) but have no publications associated with them.
gThese negative stain electron microscopy structures have resolutions of 16–30 Å, thus provide approximate envelopes for fitting high-resolution crystallographic or modeled structures.