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Solution structure of the calmodulin‐like C ‐terminal domain of Entamoeba α‐actinin2
Author(s) -
Karlsson Göran,
Persson Cecilia,
Mayzel Maxim,
Hedenström Mattias,
Backman Lars
Publication year - 2016
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24992
Subject(s) - entamoeba histolytica , calmodulin , linker , actin , entamoeba , motility , protein filament , microbiology and biotechnology , chemistry , cytoskeleton , binding domain , ef hand , terminal (telecommunication) , biophysics , biology , cell , biochemistry , binding site , computer science , telecommunications , enzyme , operating system
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 α‐actinin has been implied in several important cellular processes. In Entamoeba histolytica , the etiological agent of human amoebiasis, α‐actinin is believed to be required for infection. To better understand the role of α‐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. © 2016 Wiley Periodicals, Inc.