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TitleOpening of tandem calponin homology domains regulates their affinity for F-actin.
Journal, issue, pagesNat Struct Mol Biol, Vol. 17, Issue 5, Page 614-616, Year 2010
Publish dateApr 11, 2010
AuthorsVitold E Galkin / Albina Orlova / Anita Salmazo / Kristina Djinovic-Carugo / Edward H Egelman /
PubMed AbstractMany actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH ...Many actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH domains of alpha-actinin to be in a compact, closed conformation, but the interpretations of complexes of such tandem CH domains with F-actin have been ambiguous. We show that the tandem CH domains of alpha-actinin bind F-actin in an open conformation, explaining mutations that cause human diseases and suggesting that the opening of these domains may be one of the main regulatory mechanisms for proteins with tandem CH domains.
External linksNat Struct Mol Biol / PubMed:20383143 / PubMed Central
MethodsEM (helical sym.)
Resolution15.0 Å
Structure data

5170

3lue

EMDB-5170: Binding of alpha-actinin CH1 to F-actin
PDB-3lue: Model of alpha-actinin CH1 bound to F-actin
Method: EM (helical sym.) / Resolution: 15.0 Å

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / calponin homology domains / Acetylation / ATP-binding / Cytoplasm / Cytoskeleton / Methylation / Nucleotide-binding / Phosphoprotein / Actin-binding / Calcium / Polymorphism / Deafness / Disease mutation / Dystonia

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