Fabry disease: Identification of 50 novel α-galactosidase A mutations causing the classic phenotype and three-dimensional structural analysis of 29 missense mutations

Table 3 Predicted structural alterations caused by the novel missense mutation.

Residue	Fabry mutation	Importance in *α-Gal A*	Residue/side-chain accessible surface (Ǻ²)	Solvent exposure of residue
N34	K	Disrupts hydrogen bonding	42.83/18.23	Buried
T41	I	Buried, lines active site	8.87/2.18	Buried
D93	V	Active site; prevents substrate binding	2.38/2.38	Buried
R112	S	Misfolding	19.69/15.48	Buried
L166	G	Active site; prevents substrate binding	4.19/4.19	Buried
G171	D	Active site; prevents substrate binding	3.04/0.00	Buried
M187	T	Misfolding	0.05/0.05	Buried
S201	Y	Active site, prevents substrate binding	7.71/7.71	Buried
	F	Active site; prevents substrate binding
D234	E	Dimer interface; disrupts dimer association	1.44/0.84	Buried
W236	R	Dimer interface; buries acharge	20.31/18.66	Buried
D264	Y	Active site; prevents substrate binding	12.79/11.00	Buried
M267	R	Misfolding; buries charge	4.87/3.78	Buried
V269	M	Misfolding	1.76/0.00	Buried
G271	V	Misfolding; phi/psi constraints	15.13/0.00	Intermediate
	S	Misfolding; phi/psi constraints
S276	G	Misfolding; loss of hydrogen bonding	5.32/3.27	Buried
Q283	P	Misfolding	0.00/0.00	Buried
A285	P	Misfolding	0.01/0.01	Buried
	D	Misfolding, buries charge
M290	I	Misfolding	3.29/3.10	Buried
P293	T	Misfolding	1.71/0.01	Buried
Q312	H	Unknown	40.14/28.62	Intermediate
Q321	R	Misfolding, disrupts hydrogen bonding	39.66/33.15	Intermediate
G328	V	Misfolding	0.83/0.00	Buried
E338	K	Unknown	5.92/5.42	Buried
A348	P	Misfolding	7.98/7.45	Buried
E358	A	Misfolding; loss of charge	33.13/28.70	Intermediate
Q386	P	Misfolding	12.93/12.93	Buried

ISSN: 1479-7364