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Solution structure of tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1

Kun Dai1, Shanhui Liao, Jiahai Zhang

  • 1Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.

Plos One
|July 19, 2011
PubMed
Abstract

Insights

The tensin2 SH2 domain

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Src homology 2 (SH2) domains are crucial for biological processes.
  • Tensin family members, including tensin2, are implicated in tumor suppression through interactions with DLC-1.
  • Understanding the tensin2 SH2 domain structure and its binding to DLC-1 is key to novel binding mode discovery.

Purpose of the Study:

  • To elucidate the three-dimensional structure of the tensin2 SH2 domain.
  • To investigate the binding mechanism between the tensin2 SH2 domain and its ligand, DLC-1.
  • To explore potential novel binding modes involving the tensin2 SH2 domain.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the solution structure of the tensin2 SH2 domain.
  • Structural analysis of the tensin2 SH2 domain was performed.
  • Ligand interaction studies were conducted to understand binding characteristics.

Main Results:

  • The tensin2 SH2 domain exhibits a conserved SH2 fold comprising five β-strands and two α-helices.
  • Unlike most SH2 domains, the tensin2 SH2 domain interacts with both non-phosphorylated and phosphorylated ligands.
  • The study identified DLC-1 as a ligand interacting with the tensin2 SH2 domain.

Conclusions:

  • The solution structure of the tensin2 SH2 domain was successfully determined using NMR spectroscopy.
  • The interactions between the tensin2 SH2 domain and its ligands occur in a phosphotyrosine-independent manner.
  • This phosphotyrosine-independent binding mode represents a novel interaction mechanism for SH2 domains.

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