transparent gif

 

Ej inloggad.

Göteborgs universitets publikationer

Solution structure of the calmodulin-like C-terminal domain of Entamoeba-actinin2

Författare och institution:
B Göran Karlsson (Svenskt NMR-centrum vid Göteborgs universitet); Cecilia Persson (Svenskt NMR-centrum vid Göteborgs universitet); Maxim Mayzel (Svenskt NMR-centrum vid Göteborgs universitet); M. Hedenstrom (-); L. Backman (-)
Publicerad i:
Proteins-Structure Function and Bioinformatics, 84 ( 4 ) s. 461-466
ISSN:
0887-3585
Publikationstyp:
Artikel, refereegranskad vetenskaplig
Publiceringsår:
2016
Språk:
engelska
Fulltextlänk:
Sammanfattning (abstract):
Cell motility is dependent on a dynamic meshwork of actin filaments that is remodelled continuously. A large number of associated proteins that are severs, cross-links, or caps the filament ends have been identified and the actin cross-linker -actinin has been implied in several important cellular processes. In Entamoeba histolytica, the etiological agent of human amoebiasis, -actinin is believed to be required for infection. To better understand the role of -actinin in the infectious process we have determined the solution structure of the C-terminal calmodulin-like domain using NMR. The final structure ensemble of the apo form shows two lobes, that both resemble other pairs of calcium-binding EF-hand motifs, connected with a mobile linker. Proteins 2016; 84:461-466.
Ämne (baseras på Högskoleverkets indelning av forskningsämnen):
NATURVETENSKAP ->
Kemi
Nyckelord:
alpha-actinin, structure, calcium-binding proteins, alpha-actinin gene, skeletal-muscle, histolytica, system, evolution, spectrin, cloning, lectin, model, Biochemistry & Molecular Biology
Postens nummer:
236864
Posten skapad:
2016-05-24 13:16

Visa i Endnote-format

Göteborgs universitet • Tel. 031-786 0000
© Göteborgs universitet 2007