Table II.
Cation-binding sites in the β1 and β3 A domains and their coordinating residues. Cation-binding site mutants made in β1 are shown in bold. Mutations were based on β3 structure as identified in the aVβ3 crystal structures. The cation-coordinating residues in β3 are shown alongside the corresponding residues in β1. Coordinating residues found only in the unliganded structure are marked with ‘*’ (12) and those found only in the liganded structure are marked with ‘**’ (13).
| Cation binding site |
Residues | |||||
|---|---|---|---|---|---|---|
| MIDAS | β3 | Asp119 | Ser121 | Ser123 | Glu220 | Asp251 |
| β1 | Asp130 | Ser132 | Ser134 | Glu229 | Asp259 | |
| mutation | D130A | |||||
| ADMIDAS | β3 | Ser123 | Asp126 | Asp127 | Met335* | Asp251** |
| β1 | Ser134 | Asp137 | Asp138 | Ala341 | Asp259 | |
| mutation | D137A | D138A | ||||
| LIMBS | β3 | Asp158 | Asn215 | Asp217 | Pro219 | Glu220 |
| β1 | Glu169 | Asn224 | Asp226 | Pro228 | Glu229 | |
| mutation |
E169A
E169D |
D226A | ||||