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Comparative study of structural changes caused by different substitutions at the same residue on α-galactosidase A.
[fabry disease]
Missense
mutations
in
the
α-galactosidase
A
(
GLA
)
gene
comprising
the
majority
of
mutations
responsible
for
Fabry
disease
result
in
heterogeneous
phenotypes
ranging
from
the
early
onset
severe
"
classic
"
form
to
the
"
later-onset
"
milder
form
.
To
elucidate
the
molecular
basis
of
Fabry
disease
from
the
viewpoint
of
structural
biology
,
we
comprehensively
examined
the
effects
of
different
substitutions
at
the
same
residue
in
the
amino
acid
sequence
of
GLA
on
the
structural
change
in
the
enzyme
molecule
and
the
clinical
phenotype
by
calculating
the
number
of
atoms
affected
and
the
root-mean-square-distance
value
,
and
by
coloring
of
the
atoms
influenced
by
the
amino
acid
replacements
.
The
results
revealed
that
the
severity
of
the
structural
change
influences
the
disease
progression
,
i
.
e
.
,
a
small
structural
change
tends
to
lead
to
the
later-onset
form
and
a
large
one
to
the
classic
form
.
Furthermore
,
the
study
revealed
the
residues
important
for
expression
of
the
GLA
activity
,
i
.
e
.
,
residues
involved
in
construction
of
the
active
site
,
a
disulfide
bond
or
a
dimer
.
Structural
study
from
such
a
viewpoint
is
useful
for
elucidating
the
basis
of
Fabry
disease
.