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3lue
From Proteopedia
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[[Image:3lue.png|left|200px]] | [[Image:3lue.png|left|200px]] | ||
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{{STRUCTURE_3lue| PDB=3lue | SCENE= }} | {{STRUCTURE_3lue| PDB=3lue | SCENE= }} | ||
===Model of alpha-actinin CH1 bound to F-actin=== | ===Model of alpha-actinin CH1 bound to F-actin=== | ||
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{{ABSTRACT_PUBMED_20383143}} | {{ABSTRACT_PUBMED_20383143}} | ||
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==See Also== | ==See Also== | ||
| - | *[[Actin]] | + | *[[Actin|Actin]] |
| - | *[[Actinin]] | + | *[[Actinin|Actinin]] |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020383143</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Djinovic-Carugo, K.]] | [[Category: Djinovic-Carugo, K.]] | ||
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[[Category: Orlova, A.]] | [[Category: Orlova, A.]] | ||
[[Category: Salmazo, A.]] | [[Category: Salmazo, A.]] | ||
| - | [[Category: Acetylation]] | ||
[[Category: Actin-binding]] | [[Category: Actin-binding]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
| - | [[Category: Calcium]] | ||
[[Category: Calponin homology domain]] | [[Category: Calponin homology domain]] | ||
| - | [[Category: Cytoplasm]] | ||
[[Category: Cytoskeleton]] | [[Category: Cytoskeleton]] | ||
[[Category: Deafness]] | [[Category: Deafness]] | ||
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[[Category: Nucleotide-binding]] | [[Category: Nucleotide-binding]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
| - | [[Category: Polymorphism]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] | ||
Revision as of 10:19, 26 July 2012
Contents |
Model of alpha-actinin CH1 bound to F-actin
Template:ABSTRACT PUBMED 20383143
About this Structure
3lue is a 20 chain structure of Actin and Actinin with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Galkin VE, Orlova A, Salmazo A, Djinovic-Carugo K, Egelman EH. Opening of tandem calponin homology domains regulates their affinity for F-actin. Nat Struct Mol Biol. 2010 May;17(5):614-6. Epub 2010 Apr 11. PMID:20383143 doi:10.1038/nsmb.1789
