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-Structure paper
| タイトル | Opening of tandem calponin homology domains regulates their affinity for F-actin. |
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| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 17, Issue 5, Page 614-616, Year 2010 |
| 掲載日 | 2010年4月11日 |
著者 | Vitold E Galkin / Albina Orlova / Anita Salmazo / Kristina Djinovic-Carugo / Edward H Egelman / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Nat Struct Mol Biol / PubMed:20383143 / PubMed Central |
| 手法 | EM (らせん対称) |
| 解像度 | 15.0 Å |
| 構造データ | |
| 由来 |
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キーワード | STRUCTURAL 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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