3LUE

Model of alpha-actinin CH1 bound to F-actin

Summary for 3LUE

• Entry DOI: 10.2210/pdb3lue/pdb
• EMDB information: 5170
• Descriptor: Actin, cytoplasmic 1, Alpha-actinin-3 (2 entities in total)
• Functional Keywords: calponin homology domains, acetylation, atp-binding, cytoplasm, cytoskeleton, methylation, nucleotide-binding, phosphoprotein, actin-binding, calcium, polymorphism, structural protein, deafness, disease mutation, dystonia
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 20
• Total formula weight: 541231.77

Authors

Galkin, V.E.,Orlova, A.,Salmazo, A.,Djinovic-Carugo, K.,Egelman, E.H. (deposition date: 2010-02-17, release date: 2010-04-28, Last modification date: 2024-02-21)

Primary citation

Galkin, V.E.,Orlova, A.,Salmazo, A.,Djinovic-Carugo, K.,Egelman, E.H.
Opening of tandem calponin homology domains regulates their affinity for F-actin.
Nat.Struct.Mol.Biol., 17:614-616, 2010

PubMed Abstract: 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.

PubMed: 20383143
DOI: 10.1038/nsmb.1789

Experimental method

ELECTRON MICROSCOPY (15 Å)