Conservation of Short Linear Motifs in Disordered Protein Regions
Author Information
Author(s): Ren Siyuan, Uversky Vladimir N, Chen Zhengjun, Dunker A Keith, Obradovic Zoran
Primary Institution: Center for Information Science and Technology, Temple University
Hypothesis
SLiMs recognized by SH2, SH3, and Ser/Thr Kinase domains are more conserved in disordered regions than in ordered regions.
Conclusion
Functional SLiMs recognized by each domain occur more often in disordered compared to structured regions of proteins.
Supporting Evidence
- SLiMs in disordered regions exhibit greater conservation than their flanking sequences.
- SLiMs recognized by SH2 domains are more likely to bind in disordered regions.
- Conservation profiles indicate that frequent binding partners show higher conservation signals.
Takeaway
Some parts of proteins can change shape and are more flexible, which helps them interact better with other proteins. This study found that these flexible parts are often more similar across different species.
Methodology
The study analyzed the evolutionary conservation of SLiMs in ordered and disordered protein regions using sequence data from various databases and disorder prediction methods.
Limitations
The study is limited to specific domains and may not represent all SLiMs across different proteins.
Participant Demographics
Human proteins were selected based on specific criteria from the SwissProt database.
Statistical Information
P-Value
p<0.001
Statistical Significance
p<0.001
Digital Object Identifier (DOI)
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