1MB8

Crystal Structure of the actin binding domain of plectin

Summary for 1MB8

• Entry DOI: 10.2210/pdb1mb8/pdb
• Descriptor: Plectin (2 entities in total)
• Functional Keywords: calponin homology domain, actin binding domain, integrin beta4 hemidesmosomes, cytoskeleton, epidermolysis bullosa, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton: Q15149
• Total number of polymer chains: 1
• Total formula weight: 28444.57

Authors

de Pereda, J.M. (deposition date: 2002-08-02, release date: 2003-06-10, Last modification date: 2024-02-14)

Primary citation

Garcia-Alvarez, B.,Bobkov, A.,Sonnenberg, A.,de Pereda, J.M.
Structural and Functional Analysis of the Actin Binding Domain of Plectin Suggests Alternative Mechanisms for Binding to F-Actin and Integrin Beta4
Structure, 11:615-625, 2003

PubMed Abstract: Plectin is a widely expressed cytoskeletal linker. Here we report the crystal structure of the actin binding domain of plectin and show that this region is sufficient for interaction with F-actin or the cytoplasmic region of integrin alpha6beta4. The structure is formed by two calponin homology domains arranged in a closed conformation. We show that binding to F-actin induces a conformational change in plectin that is inhibited by an engineered interdomain disulfide bridge. A two-step induced fit mechanism involving binding and subsequent domain rearrangement is proposed. In contrast, interaction with integrin alpha6beta4 occurs in a closed conformation. Competitive binding of plectin to F-actin and integrin alpha6beta4 may rely on the observed alternative binding mechanisms and involve both allosteric and steric factors.

PubMed: 12791251
DOI: 10.1016/S0969-2126(03)00090-X

Experimental method

X-RAY DIFFRACTION (2.15 Å)