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Fnbp1  -  formin binding protein 1

Mus musculus

Synonyms: 1110057E06Rik, 2210010H06Rik, FBP1, FBP17, Fbp17, ...
 
 
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High impact information on Fnbp1

  • The 37-residue Formin-binding protein, FBP28, is a canonical three-stranded beta-sheet WW domain [1].
  • We showed previously that PDE6gamma is able to interact with the Src-homology type 3 (SH3) domain of formin-binding protein 17 (FBP17), a protein involved in membrane receptor endocytosis [2].
  • Mutational analysis of the Pgamma-rod-FBP17 interaction confirmed it involved the proline-rich domain of Pgamma-rod and the SH3 domain of FBP17 [3].
 

Biological context of Fnbp1

  • METHODS: Several SH3 domains highly homologous to this domain of FBP17 were found by structural alignment [2].

References

  1. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R. J. Mol. Biol. (2006) [Pubmed]
  2. The regulatory subunit of PDE6 interacts with PACSIN in photoreceptors. Houdart, F., Girard-Nau, N., Morin, F., Voisin, P., Vannier, B. Mol. Vis. (2005) [Pubmed]
  3. A proline-rich domain in the gamma subunit of phosphodiesterase 6 mediates interaction with SH3-containing proteins. Morin, F., Vannier, B., Houdart, F., Regnacq, M., Berges, T., Voisin, P. Mol. Vis. (2003) [Pubmed]
 
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