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PDBsum entry 3f7p
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Structural protein/cell adhesion
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PDB id
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3f7p
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Contents |
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231 a.a.
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200 a.a.
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212 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Structural protein/cell adhesion
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Title:
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Crystal structure of a complex between integrin beta4 and plectin
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Structure:
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Plectin-1. Chain: a, b. Fragment: actin-binding domain, residues 1-293. Synonym: plectin 1c, pltn, pcn, hemidesmosomal protein 1, hd1, plectin-6, plectin-11. Engineered: yes. Integrin beta-4. Chain: c, d, e. Fragment: fibronectin type-iii, residues 1126-1370.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: plec-1 (isoform 1c), plec1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: itgb4.
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Resolution:
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2.75Å
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R-factor:
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0.207
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R-free:
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0.257
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Authors:
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J.M.De Pereda
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Key ref:
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J.M.de Pereda
et al.
(2009).
Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes.
Embo J,
28,
1180-1190.
PubMed id:
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Date:
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10-Nov-08
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Release date:
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10-Mar-09
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PROCHECK
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Headers
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References
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Q15149
(PLEC_HUMAN) -
Plectin from Homo sapiens
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Seq:
Struc:
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4684 a.a.
231 a.a.*
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Embo J
28:1180-1190
(2009)
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PubMed id:
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Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes.
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J.M.de Pereda,
M.P.Lillo,
A.Sonnenberg.
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ABSTRACT
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The interaction between the integrin alpha6beta4 and plectin is essential for
the assembly and stability of hemidesmosomes, which are junctional adhesion
complexes that anchor epithelial cells to the basement membrane. We describe the
crystal structure at 2.75 A resolution of the primary alpha6beta4-plectin
complex, formed by the first pair of fibronectin type III domains and the
N-terminal region of the connecting segment of beta4 and the actin-binding
domain of plectin. Two missense mutations in beta4 (R1225H and R1281W) linked to
nonlethal forms of epidermolysis bullosa prevent essential intermolecular
contacts. We also present two structures at 1.75 and 2.05 A resolution of the
beta4 moiety in the absence of plectin, which reveal a major rearrangement of
the connecting segment of beta4 on binding to plectin. This conformational
switch is correlated with the way alpha6beta4 promotes stable adhesion or cell
migration and suggests an allosteric control of the integrin.
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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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F.Yang,
A.P.West,
and
P.J.Bjorkman
(2011).
Crystal structure of a hemojuvelin-binding fragment of neogenin at 1.8Å.
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J Struct Biol,
174,
239-244.
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PDB code:
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C.Sun,
X.Liu,
L.Qi,
J.Xu,
J.Zhao,
Y.Zhang,
S.Zhang,
and
J.Miao
(2010).
Modulation of vascular endothelial cell senescence by integrin β4.
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J Cell Physiol,
225,
673-681.
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H.J.Chung,
and
J.Uitto
(2010).
Epidermolysis bullosa with pyloric atresia.
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Dermatol Clin,
28,
43-54.
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H.J.Chung,
and
J.Uitto
(2010).
Type VII collagen: the anchoring fibril protein at fault in dystrophic epidermolysis bullosa.
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Dermatol Clin,
28,
93.
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R.W.Groves,
L.Liu,
P.J.Dopping-Hepenstal,
H.S.Markus,
P.A.Lovell,
L.Ozoemena,
J.E.Lai-Cheong,
J.Gawler,
K.Owaribe,
T.Hashimoto,
J.E.Mellerio,
J.B.Mee,
and
J.A.McGrath
(2010).
A homozygous nonsense mutation within the dystonin gene coding for the coiled-coil domain of the epithelial isoform of BPAG1 underlies a new subtype of autosomal recessive epidermolysis bullosa simplex.
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J Invest Dermatol,
130,
1551-1557.
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J.M.de Pereda,
E.Ortega,
N.Alonso-García,
M.Gómez-Hernández,
and
A.Sonnenberg
(2009).
Advances and perspectives of the architecture of hemidesmosomes: lessons from structural biology.
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Cell Adh Migr,
3,
361-364.
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N.Alonso-García,
A.Inglés-Prieto,
A.Sonnenberg,
and
J.M.de Pereda
(2009).
Structure of the Calx-beta domain of the integrin beta4 subunit: insights into function and cation-independent stability.
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Acta Crystallogr D Biol Crystallogr,
65,
858-871.
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PDB codes:
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
