Rare Diseases Symptoms Automatic Extraction
Home
A random Abstract
Our Project
Our Team
Structural basis for heteromeric assembly and perinuclear organization of keratin filaments.
[epidermolysis bullosa simplex]
There
is
as
yet
no
high
-resolution
data
regarding
the
structure
and
organization
of
keratin
intermediate
filaments
,
which
are
obligate
heteropolymers
providing
vital
mechanical
support
in
epithelia
.
We
report
the
crystal
structure
of
interacting
2
B
regions
from
the
central
coiled-coil
domains
of
keratins
5
and
14
(
K
5
and
K
14
)
,
expressed
in
progenitor
keratinocytes
of
epidermis
.
The
interface
of
the
K
5
-
K
14
coiled-coil
heterodimer
has
asymmetric
salt
bridges
,
hydrogen
bonds
and
hydrophobic
contacts
,
and
its
surface
exhibits
a
notable
charge
polarization
.
A
trans-dimer
homotypic
disulfide
bond
involving
Cys
367
in
K
14
's
stutter
region
occurs
in
the
crystal
and
in
skin
keratinocytes
,
where
it
is
concentrated
in
a
keratin
filament
cage
enveloping
the
nucleus
.
We
show
that
K
14
-
Cys
367
impacts
nuclear
shape
in
cultured
keratinocytes
and
that
mouse
epidermal
keratinocytes
lacking
K
14
show
aberrations
in
nuclear
structure
,
highlighting
a
new
function
for
keratin
filaments
.
