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PMID:10561496

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Citation

Gieseler, K, Abdel-Dayem, M and Ségalat, L (1999) In vitro interactions of Caenorhabditis elegans dystrophin with dystrobrevin and syntrophin. FEBS Lett. 461:59-62

Abstract

Dystrophin, the product of the gene mutated in Duchenne muscular dystrophy (DMD) is bound by its C-terminus to a protein complex including the related protein dystrobrevin. Both proteins contain a putative coiled-coil domain consisting of two alpha-helices. It has been reported that the two proteins bind to each other by the first one of the two alpha-helices. We have revisited this question using the Caenorhabditis elegans homologs of dystrophin and dystrobrevin. In vitro interaction occurs through the more conserved second helix. We propose a new model of dystrophin interactions with associated proteins.

Links

PubMed

Keywords

Amino Acid Sequence; Animals; Caenorhabditis elegans/chemistry; Caenorhabditis elegans Proteins; Dystrophin/chemistry; Dystrophin/metabolism; Dystrophin-Associated Proteins; Glutathione Transferase/metabolism; Humans; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Models, Biological; Molecular Sequence Data; Muscle Proteins/chemistry; Muscle Proteins/metabolism; Nerve Tissue Proteins; Neuropeptides/chemistry; Neuropeptides/metabolism; Protein Binding; Protein Conformation; Recombinant Fusion Proteins/metabolism; Sequence Homology, Amino Acid

Significance

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status


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References

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