Table 2.
Disease-causing missense mutations with critical roles in protein stability.
| Protein | Retrieved mutations | Missense mutations mapped onto structural domains | Unfolding fraction per domain | Number of mutations with critical roles predicted in silico |
|---|---|---|---|---|
| EYS | 155 | 101 | 0.78 ± 0.26 | 42 (42%) |
| FBN1 | 1580 | 1451 | 0.75 ± 0.22 | 834 (57%) |
| FBN2 | 64 | 60 | 0.70 ± 0.27 | 27 (45%) |
| CFH | 219 | 214 | 0.71 ± 0.24 | 70 (33%) |
| PCDH15 | 60 | 46 | 0.70 ± 0.30 | 11 (24%) |
| FAT1 | 20 | 15 | 0.62 ± 0.24 | 3 (20%) |
| FAT4 | 23 | 23 | 0.71 ± 0.28 | 3 (13%) |
| ROBO3 | 21 | 19 | 0.82 ± 0.22 | 9 (47%) |
| CDH23 | 234 | 218 | 0.59 ± 0.26 | 29 (13%) |
From left to right: protein name; number of mutations retrieved from HGMD; number and average unfolding fraction of disease-causing mutations associated with structural domains, and number and percentage of HGMD mutations with critical roles (unfolding fraction > 0.9).