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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of Molecular...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of Molecular Biology
Article . 2003 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
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Isolation of Proteins that Interact with the Signal Transduction Molecule Dof and Identification of a Functional Domain Conserved between Dof and Vertebrate BCAP

Authors: Alysia, Battersby; Agnes, Csiszár; Maria, Leptin; Robert, Wilson;

Isolation of Proteins that Interact with the Signal Transduction Molecule Dof and Identification of a Functional Domain Conserved between Dof and Vertebrate BCAP

Abstract

Dof is a large molecule essential for signal transduction by the two FGF receptors in Drosophila. It contains two ankyrin repeats and a coiled-coil region, but has no other recognisable structural motif. Dof shares these features with its closest vertebrate relatives, the B-cell signalling molecules BCAP and BANK. In addition, this family of proteins shares a region of homology upstream of the ankyrin repeats, which we call the Dof/BCAP/BANK (DBB) motif. We have identified 44 proteins that interact with Dof in a yeast two-hybrid screen. These include the Drosophila FGF-receptor Heartless and Dof itself. We show that the integrity of the DBB motif is required both for Dof and for BCAP to form dimers. Analysis of the interactions between a set of deletion constructs of Dof and the panel of interactors suggests that Dof may adopt different conformations, with a folded conformation stabilized by interactions between the DBB motif and the C-terminal part of the protein.

Related Organizations
Keywords

Binding Sites, Amino Acid Motifs, Molecular Sequence Data, Gene Expression Regulation, Developmental, Membrane Proteins, Receptors, Fibroblast Growth Factor, Protein Structure, Tertiary, Animals, Drosophila Proteins, Insect Proteins, Drosophila, Amino Acid Sequence, RNA, Messenger, Carrier Proteins, Dimerization, Cells, Cultured, Conserved Sequence, In Situ Hybridization, Adaptor Proteins, Signal Transducing, Protein Binding

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Powered by OpenAIRE graph
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
31
Average
Top 10%
Top 10%