Solution Structure of Tensin2 SH2 Domain and Its Phosphotyrosine-Independent Interaction with DLC-1
2011
Structure of Tensin2 SH2 Domain and Its Interaction with DLC-1
publication
Evidence: high
Author Information
Author(s): Dai Kun, Liao Shanhui, Zhang Jiahai, Zhang Xuecheng, Tu Xiaoming
Primary Institution: University of Science and Technology of China
Hypothesis
What is the structure of tensin2 SH2 domain and how does it bind to DLC-1?
Conclusion
The tensin2 SH2 domain interacts with DLC-1 in a phosphotyrosine-independent manner.
Supporting Evidence
- Tensin2 SH2 domain adopts a conserved SH2 fold consisting of five β-strands and two α-helices.
- Tensin2 SH2 domain was shown to bind both phosphorylated and nonphosphorylated DLC-1 peptides.
- The interaction of tensin2 SH2 domain with DLC-1 is relatively phosphorylation independent.
Takeaway
This study found that a part of a protein called tensin2 can stick to another protein called DLC-1 without needing a special chemical tag, which is usually required for such interactions.
Methodology
The solution structure of tensin2 SH2 domain was determined using NMR spectroscopy, and interactions were analyzed using surface plasmon resonance.
Digital Object Identifier (DOI)
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