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Three dimensional structure of the closed conformation (active) of human merlin reveals masking of actin binding site in the FERM domainPublished in
2009
PMID: 19778867
Volume: 5
Issue: 5
Pages: 516 - 524
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. Copyright © 2009 Inderscience Enterprises Ltd.
Topics: FERM domain (65)%65% related to the paper, Merlin (protein) (55)%55% related to the paper, Ezrin (54)%54% related to the paper and Binding site (51)%51% related to the paper
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About the journal
| Journal | International Journal of Bioinformatics Research and Applications |
|---|---|
| ISSN | 17445485 |
| Open Access | No |
Authors (1)
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Concepts (40)
ACTIN- Arginine
- Asparagine
- Glutamic acid
- Glutamine
- Leucine
- MERLIN
- Methionine
- MOESIN
- Proline
- SPECTRIN
- SPECTRIN BETA 2
- Tryptophan
- Tyrosine
- Unclassified drug
- Valine
- Alpha helix
- Article
- Binding site
- Carboxy terminal sequence
- Computer model
- Human
- LEPIDOPTERA
- Nonhuman
- Protein binding
- Protein conformation
- Protein domain
- Protein protein interaction
- Protein structure
- Sequence homology
- Actins
- Binding sites
- Catalytic domain
- Computational biology
- Humans
- Models, molecular
- NEUROFIBROMIN 2
- Protein folding
- Protein structure, tertiary
- SPODOPTERA FRUGIPERDA
