How Two Domains of Protein Tyrosine Phosphatases Work Together
Author Information
Author(s): Madan Lalima L., Veeranna S., Shameer Khader, Reddy Chilamakuri C. S., Sowdhamini R., Gopal B.
Primary Institution: Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
Hypothesis
The D2 domain of receptor protein tyrosine phosphatases influences the catalytic activity and substrate specificity of the D1 domain.
Conclusion
The D2 domain can either inhibit or enhance the catalytic activity of the D1 domain depending on the specific protein.
Supporting Evidence
- The D2 domain of DLAR decreases the activity of its D1 domain.
- The D2 domain of PTP99A increases the activity of its D1 domain.
- Substrate specificity is influenced by both D1 and D2 domains.
Takeaway
This study shows that parts of proteins can work together in surprising ways, either helping or hurting each other's function.
Methodology
The study used biochemical assays and molecular dynamics simulations to analyze the interactions between the D1 and D2 domains of two receptor protein tyrosine phosphatases.
Limitations
The study primarily focuses on two specific proteins and may not generalize to all protein tyrosine phosphatases.
Digital Object Identifier (DOI)
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