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Once established, a SLiM binding pocket is generally conserved over large evolutionary distances as the motif partners constrain the pocket (unless the domain duplicates).
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Results: In this article, interaction data are analysed to identify and characterize an important subset of PPIs, those involving SLiMs binding to globular domains.
Another example is the analogy of SLiM-binding pocket and SLiM co-evolution with DNA-binding domain - DNA regulatory element co-evolution.
A significant portion of the higher eukaryotic motif space (the set of motifs with the ability to specifically bind a SLiM-binding pocket) is now utilised by SLiM-binding domain families [ 9, 88– 90].
The datasets were split into training and test datasets and assessed for sensitivity and specificity: The true hits are considered correct if the annotated SLiM and SLiM-binding domain positions were predicted to bind with a score above the set threshold.
iELM, so far, covers only linear motifs as they are annotated in the ELM resource, but is easily extendible to any SLiM, in the form of a regular expression, for which the interacting SLiM-binding domain is known.
By incorporating known binding specificities, those HMMs trained to recognize SLiM-binding domain should distinguish the subgroups of those functional globular domains that bind multiple ELM classes (see Supplementary Material for details).
The sporadic evolution of novel motif-binding pockets in domains that previously had no SLiM-binding ability has contributed to the diversity of SLiM-binding [ 73, 74].
A dataset of SLiM-binding domains and SLiM-mediated interactions was manually curated from the literature.
To identify the remaining 72% (112) of SLiM-binding domains a literature search was undertaken.
This requires a PDB structure (or a model) of the putative SLiM-binding domain.
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