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Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
Structural conservation of a short, functional, peptide-sequence motif
Susan Fox-Erlich1, Martin R Schiller, Michael R Gryk
1Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3305, USA.
Frontiers in Bioscience (Landmark Edition)
|March 11, 2009
Summary
Bioinformatic tools help identify protein domains and short linear motifs crucial for protein interactions. Understanding these sequences, often in unstructured regions, aids in deciphering protein function and structure.
Area of Science:
- Molecular Biology
- Bioinformatics
- Structural Biology
Background:
- Eukaryotic proteins comprise multiple autonomously folding domains.
- Protein domains recognize short, linear amino acid sequences on partner proteins for binding and modification.
- These interactions are fundamental to cellular processes.
Purpose of the Study:
- To review bioinformatic tools for discovering and cataloging protein domains.
- To survey tools for identifying short linear motifs (SLiMs) involved in domain targeting.
- To explore the role of protein structure in SLiM activity.
Main Methods:
- Literature review of bioinformatic tools and resources.
- Analysis of databases like the Protein Data Bank (PDB) for protein structures.
- Examination of the relationship between SLiMs and protein structure.
Main Results:
- Numerous bioinformatic tools exist for protein domain and SLiM identification.
- SLiMs are often located in intrinsically disordered protein regions.
- Protein structure plays a role in the function of certain SLiMs.
Conclusions:
- Bioinformatic resources are essential for understanding protein domain and SLiM biology.
- Further research into SLiM structure-function relationships is warranted.
- Integrating structural data with motif analysis enhances our understanding of protein interactions.
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