TABLE 2.
Surface accessibility in the modeled CD81 structure of tetraspanin residues involved in posttranslational modification and ligand binding
| CD81 residue | Corresponding residue in other tetraspanin | Accessible surface (Å2) | Accessibility criteria | Reference |
|---|---|---|---|---|
| C6 | – | 52.2 | Palmitoylation | 12 |
| C9 | – | 49.8 | Palmitoylation | 12 |
| K52* | N51 (CD9) | 96.5 | N-glycosylation | 79 |
| P53* | N52 (CD9) | 27.3 | N-glycosylation | 79 |
| C80 | – | 23.0 | Palmitoylation | 12 |
| Y81* | C80 (CD151) | 139.3 | Palmitoylation | 12 |
| C89 | – | 102.5 | Palmitoylation | 12 |
| D138* | N129 (CD53, CD63) | 106.0 | N-glycosylation | 16 |
| N141* | C151(peripherin) | 97.8 | Intermolecular disulfide | 13 |
| L162 | – | 28.5 | HCV glycoprotein E2 binding | 80 |
| T163 | – | 79.5 | HCV glycoprotein E2 binding | 15 |
| I182 | – | 114.5 | HCV glycoprotein E2 binding | 80 |
| N184 | – | 17.6 | HCV glycoprotein E2 binding | 80 |
| F186 | – | 140.5 | HCV glycoprotein E2 binding | 15 |
| D196 | – | 50.8 | HCV glycoprotein E2 binding | 15 |
| M224* | C242 (CD151) | 88.2 | Palmitoylation | 12 |
| V225* | C243 (CD151) | 64.0 | Palmitoylation | 12 |
| C227 | – | 28.3 | Palmitoylation | 12 |
| C228 | – | 74.7 | Palmitoylation | 12 |
In the first column, residues without asterisks are known to be accessible in CD81 whereas those with an asterisk are CD81 residues corresponding sequentially to residues known to be accessible in other tetraspanins and listed in the second column. Accessible surface includes side chain and Cα.