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Sivakumar, K C. (2009) Three dimensional structure of the closed conformation (active) of human merlin reveals masking of actin binding site in the FERM domain. International journal of bioinformatics research and applications, 5 (5). pp. 516-24. ISSN 1744-5493

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We modelled the structure of human merlin using the structure of moesin from Spodoptera frugiperda as the template. The present model suggests an interaction of its extreme C-terminal region with the subdomains B and C of FERM domain, masking the binding site of beta II spectrin. Modelling the complete structure of merlin revealed a novel central alpha helical domain with a helix-coil-helix. The actin binding site in the carboxy terminal is absent in merlin and in its closed conformation the indirect actin binding site in the FERM domain is also not available for the interaction of other proteins with it.

Item Type: Article
Uncontrolled Keywords: : ezrin, moesin proteins, radixin proteins, human merlin, neurofibromatosis, betaII spectrin, modelling, tumour suppressor, actin binding, bioinformatics, FERM, closed conformation
Subjects: Human Molecular Genetics
Depositing User: Rgcb Library
Date Deposited: 23 Oct 2019 09:26
Last Modified: 23 Oct 2019 09:27
URI: http://rgcb.sciencecentral.in/id/eprint/891

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