Search results for "Short linear motif"

Supramolecular polymerization of electronically complementary linear motifs: anti-cooperativity by attenuated growth†

2021

Anti-cooperative supramolecular polymerization by attenuated growth exhibited by self-assembling units of two electron-donor benzo[1,2-b:4,5-b′]dithiophene (BDT) derivatives (compounds 1a and 1b) and the electron-acceptor 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene (BODIPY) (compound 2) is reported. Despite the apparent cooperative mechanism of 1 and 2, AFM imaging and SAXS measurements reveal the formation of small aggregates that suggest the operation of an anti-cooperative mechanism strongly conditioned by an attenuated growth. In this mechanism, the formation of the nuclei is favoured over the subsequent addition of monomeric units to the aggregate, which finally results in short aggrega…

Author response: Inhibitory activities of short linear motifs underlie Hox interactome specificity in vivo

2015

Inhibitory activities of short linear motifs underlie Hox interactome specificity in vivo

2015

Hox proteins are well-established developmental regulators that coordinate cell fate and morphogenesis throughout embryogenesis. In contrast, our knowledge of their specific molecular modes of action is limited to the interaction with few cofactors. Here, we show that Hox proteins are able to interact with a wide range of transcription factors in the live Drosophila embryo. In this context, specificity relies on a versatile usage of conserved short linear motifs (SLiMs), which, surprisingly, often restrains the interaction potential of Hox proteins. This novel buffering activity of SLiMs was observed in different tissues and found in Hox proteins from cnidarian to mouse species. Although th…

Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2

2016

We show that a peptide from Chikungunya virus nsP3 protein spanning residues 1728–1744 binds the amphiphysin-2 (BIN1) Src homology-3 (SH3) domain with an unusually high affinity (Kd 24 nM). Our NMR solution complex structure together with isothermal titration calorimetry data on several related viral and cellular peptide ligands reveal that this exceptional affinity originates from interactions between multiple basic residues in the target peptide and the extensive negatively charged binding surface of amphiphysin-2 SH3. Remarkably, these arginines show no fixed conformation in the complex structure, indicating that a transient or fluctuating polyelectrostatic interaction accounts for this …