3F7R

First pair of Fibronectin type III domains and part of the connecting segment of the integrin beta4

Summary for 3F7R

• Entry DOI: 10.2210/pdb3f7r/pdb
• Related: 1QG3 3F7P 3F7Q
• Descriptor: Integrin beta-4, CHLORIDE ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: integrin, hemidesmosome, cell adhesion, carcinoma, epidermolysis bullosa, alternative splicing, disease mutation, glycoprotein, membrane, phosphoprotein, polymorphism, receptor, transmembrane
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P16144
• Total number of polymer chains: 1
• Total formula weight: 27905.63

Authors

de Pereda, J.M. (deposition date: 2008-11-10, release date: 2009-03-10, Last modification date: 2023-11-01)

Primary citation

de Pereda, J.M.,Lillo, M.P.,Sonnenberg, A.
Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes
Embo J., 28:1180-1190, 2009

PubMed Abstract: 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.

PubMed: 19242489
DOI: 10.1038/emboj.2009.48

Experimental method

X-RAY DIFFRACTION (2.036 Å)