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Novel structural insights into F-actin-binding and novel functions of calponin homology domains

Authors
Journal
Current Opinion in Structural Biology
0959-440X
Publisher
Elsevier
Publication Date
Volume
18
Issue
6
Identifiers
DOI: 10.1016/j.sbi.2008.10.003

Abstract

Tandem calponin homology (CH) domains are well-known actin filaments (F-actin) binding motifs. There has been a continuous debate about the details of CH domain–actin interaction, mainly because atomic level structures of F-actin are not available. A recent electron microscopy study has considerably advanced our structural understanding of CH domain:F-actin complex. On the contrary, it has recently also been shown that CH domains can bind other macromolecular systems: two CH domains from separate polypeptides Ncd80, Nuf2 can form a microtubule-binding site, as well as tandem CH domains in the EB1 dimer, while the single C-terminal CH domain of α-parvin has been observed to bind to a α-helical leucin–aspartate rich motif from paxillin.

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