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PDBsum entry 1eu0
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Structural protein
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PDB id
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1eu0
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DOI no:
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FEBS Lett
473:127-131
(2000)
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PubMed id:
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alpha-Helical solenoid model for the human involucrin.
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A.V.Kajava.
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ABSTRACT
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Involucrin is a key component of the cross-linked envelope of terminally
differentiated keratinocytes. The human molecule largely consists of 10 residue
repeats and forms a thin 460 A long rod. Summarized experimental data and a
detailed stereochemical analysis made with computer modeling resulted in a
structural model for the involucrin molecule. The suggested structure is a
left-handed alpha-helical solenoid built of a tandem array of helix-turn-helix
folds. The structure enables us to explain the whole set of experimental data
and residue conservations within the repeats. It is ideally suited to serve as a
scaffold for cell envelope assembly and proposes a possible mode of the
intermolecular interactions of involucrin during cell cornification.
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Selected figure(s)
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Figure 1.
Fig. 1. Scheme of the repetitive multiplication of the 10
residue unit during search of the initial template for the
involucrin structure. α-Helical segments are represented by
cylinders. The crossing angle ω was used to vary the
orientation of the α-helical segments; Δz and Δφ are
components of the screw translation. Circles with ‘L’ on the
surface of the α-helices indicate location of leucines 5 and 8.
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Figure 4.
Fig. 4. Diagram showing the solvent-accessible surface of a
fragment of the repetitive domain (residues 312–361) of human
involucrin. A dotted line winding around the involucrin groove
denotes a possible mode of peptide binding. For simplicity, only
C[β] atoms of the outside side chains are shown.
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2000,
473,
127-131)
copyright 2000.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.Matsuda,
T.Koshiba,
T.Osaki,
H.Suyama,
F.Arisaka,
Y.Toh,
and
S.Kawabata
(2007).
An arthropod cuticular chitin-binding protein endows injured sites with transglutaminase-dependent mesh.
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J Biol Chem,
282,
37316-37324.
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R.L.Eckert,
M.T.Sturniolo,
A.M.Broome,
M.Ruse,
and
E.A.Rorke
(2005).
Transglutaminase function in epidermis.
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J Invest Dermatol,
124,
481-492.
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R.L.Eckert,
J.F.Crish,
T.Efimova,
S.R.Dashti,
A.Deucher,
F.Bone,
G.Adhikary,
G.Huang,
R.Gopalakrishnan,
and
S.Balasubramanian
(2004).
Regulation of involucrin gene expression.
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J Invest Dermatol,
123,
13-22.
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K.C.Madison
(2003).
Barrier function of the skin: "la raison d'être" of the epidermis.
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J Invest Dermatol,
121,
231-241.
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A.E.Kalinin,
A.V.Kajava,
and
P.M.Steinert
(2002).
Epithelial barrier function: assembly and structural features of the cornified cell envelope.
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Bioessays,
24,
789-800.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
