Understanding the Interaction of Human Formin Binding Protein 4 with Formin FMN1

  • Amit Das
  • Simanti Bhattacharya
  • Angshuman Bagchi
  • Rakhi Dasgupta
Conference paper
Part of the Advances in Intelligent Systems and Computing book series (AISC, volume 340)


The proline rich formin homolog 1 (FH1) region of mouse formin FMN1 was initially reported to bind to WW domains and mediate its interaction with formin binding protein 4 (FNBP4) via the WW domain of FNBP4. However further structural, biochemical and functional details about this interaction have never been reported. The nature of the study that first reported this interaction, along with lack of further information, later created doubt about the possibility of this interaction under cellular environment. In this context, this computational study confirms the binding of mouse formin FMN1 FH1 with the 1st WW domain of FNBP4. Combined with our previous reports, this study concludes that only the 1st WW domain of FNBP4 is able to mediate its interaction with formins FH1 regions and its binding is stronger to the PPXXPP motif compared to the PPXP or PPXPP motifs, all of which are found in formin FH1 region.


Formin FNBP4 WW domain Docking 



Formin homology


Formin binding protein


Formin 1


Mouse Diaphanous homologue 1


Proline rich ligands



AD and SB would like to thank CSIR (India) and UGC (India) respectively for their PhD fellowships. AB and RD are supported by research grants from DBT (India) (project no. BT/PR6869/BID/7/417/2013). All the authors are thankful to the Bioinformatics Infrastructure Facility (BIF), University of Kalyani for necessary computational facilities.


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Copyright information

© Springer India 2015

Authors and Affiliations

  1. 1.Department of Biochemistry and BiophysicsUniversity of KalyaniKalyani, NadiaIndia

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