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Conformation analysis of homology model of human merlin

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Author(s): Sivakumar K.C. | Vidhya Ramaswamy

Journal: International Journal of Systems Biology
ISSN 0975-2900

Volume: 2;
Issue: 1;
Start page: 12;
Date: 2010;
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Keywords: Ezrin | moesin and radixin proteins | merlin | neurofibromatosis | betaII spectrin | modelling | tumour Ezrin | moesin and radixin proteins | merlin | neurofibromatosis | betaII spectrin | modelling | tumour suppressor

ABSTRACT
Merlin shares sequence similarity with the 4.1 super family of proteins (ezrin, radixin, andmoesin) that link cell surface glycoproteins to the actin cytoskeleton. We modeled the structure of humanmerlin using the structure of moesin from Spodoptera frugiperda as the template. The present model ofmerlin structure suggests an interaction of its extreme C- terminal region with the subdomains B and C ofFERM domain, masking the binding site of beta II spectrin. Our model suggests that FERM domain ismasked in a closed conformation of merlin preventing the interaction of other proteins with it. Modeling thecomplete structure of merlin revealed a novel central alpha helical domain with a helix-coil-helix. The actinbinding site in the carboxy terminal is absent in merlin. For merlin (closed conformation), the indirect actinbinding site in the FERM domain is also not available for interaction with other proteins.
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