Nature Structural Biology9, 612 - 620 (2002)
Published online: 8 July 2002; | doi:10.1038/nsb818
Structures of two intermediate filament-binding fragments of
desmoplakin reveal a unique repeat motif structure
Hee-Jung Choi1, Shaun Park-Snyder1, Lauren T. Pascoe2, Kathleen J. Green2
& William I. Weis1
1
Departments of Structural Biology and Molecular
and Cellular Physiology, Stanford University School of Medicine,
299 Campus Drive West, Stanford,
California 94305, USA.
2
Departments of Pathology, Dermatology and the R.H.
Lurie Cancer Center, Northwestern University Medical School, 303
E. Chicago Avenue, Chicago, Illinois
60611, USA.
Desmosomes are intercellular junctions in which cadherin cell
adhesion molecules are linked to the intermediate filament (IF) system.
Desmoplakin is a member of the plakin family of IF-binding proteins. The
C-terminal domain of desmoplakin (DPCT) mediates binding to IFs in desmosomes.
The DPCT sequence contains three regions, termed A, B and C, consisting of 4.5
copies of a 38-amino acid repeat motif. We demonstrate that these regions form
discrete subdomains that bind to IFs and report the crystal structures of
domains B and C. In contrast to the elongated structures formed by other kinds
of repeat motifs, the plakin repeats form a globular structure with a unique
fold. A conserved basic groove found on the domain may represent an IF-binding
site.
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