Three dimensional structure of the closed conformation (active) of human merlin reveals masking of actin binding site in the FERM domain.
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.
Bioinformatics Centre, Rajiv Gandhi Centre for Biotechnology, Thycaud PO, Poojappura, Thiruvananthapuram, India. sivakumar@rgcb.res.in
Krishnankutty C
KC
Sivakumar
Biju
B
Thomas
Devarajan
D
Karunagaran
D000199:Actins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D020134:Catalytic Domain; D019295:Computational Biology / Q000379:methods; D006801:Humans; D008958:Models, Molecular; D025581:Neurofibromin 2 / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary
D000199:Actins; D025581:Neurofibromin 2