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Disease-causing mutation in extracellular and intracellular domain of FGFR1 protein: computational approach.
[kallmann syndrome]
In-depth
computationally
based
structural
analysis
of
human
fibroblast
growth
factor
type
1
(
FGFR
1
)
protein
carrying
disease-causing
mutation
was
performed
in
this
study
.
Gain
or
loss
of
function
due
to
missense
mutations
in
FGFR
1
is
responsible
for
a
variety
of
disorders
including
Kallmann
syndrome
,
Apert
syndrome
,
Pfeiffer
syndrome
,
Crouzon
syndrome
,
etc
.
The
mutant
model
of
the
human
FGFR
1
protein
was
subjected
to
various
in
silico
analysis
,
and
most
deleterious
SNPs
were
screened
out
.
Furthermore
,
docking
and
long
molecular
dynamics
simulations
were
carried
out
with
an
intention
of
studying
the
possible
impact
of
these
mutations
on
the
protein
structure
and
hence
its
function
.
Analysis
of
various
structural
properties-especially
of
those
of
the
functionally
important
regions
:
the
extracellular
immunoglobulin
domain
and
intracellular
Tyrosine
kinase
domain-gave
some
insights
into
the
possible
structural
characteristics
of
the
disease
mutant
and
the
wild-
type
forms
of
the
protein
.
In
a
nutshell
,
compared
to
the
wild-
type
protein
,
the
mutant
structures
V
27
3
M
and
S
685
F
are
associated
with
significant
changes
,
and
the
functionally
important
regions
seem
to
adopt
such
structures
that
are
not
conducive
for
the
wild-
type
-like
functionality
.
