Abstract:
:Alpha-actinin is the major F-actin crosslinking protein in both muscle and non-muscle cells. We report the crystal structure of the actin binding domain of human muscle alpha-actinin-3, which is formed by two consecutive calponin homology domains arranged in a "closed" conformation. Structural studies and available biochemical data on actin binding domains suggest that two calponin homology domains come in a closed conformation in the native apo-form, and that conformational changes involving the relative orientation of the two calponin homology domains are required for efficient binding to actin filaments. The actin binding activity of muscle isoforms is supposed to be regulated by phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), which binds to the second calponin homology domain. On the basis of structural analysis we propose a distinct binding site for PtdIns(4,5)P2, where the fatty acid moiety would be oriented in a direction that allows it to interact with the linker sequence between the actin binding domain and the first spectrin-like repeat, regulating thereby the binding of the C-terminal calmodulin-like domain to this linker.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Franzot G,Sjöblom B,Gautel M,Djinović Carugo Kdoi
10.1016/j.jmb.2005.01.002keywords:
subject
Has Abstractpub_date
2005-04-22 00:00:00pages
151-65issue
1eissn
0022-2836issn
1089-8638pii
S0022-2836(05)00020-3journal_volume
348pub_type
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