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

ABSTRACT: Src homology 2 (SH2) domain is a conserved module involved in various biological processes. Tensin family member was reported to be involved in tumor suppression by interacting with DLC-1 (deleted-in-liver-cancer-1) via its SH2 domain. We explore here the important questions that what the structure of tensin2 SH2 domain is, and how it binds to DLC-1, which might reveal a novel binding mode.Tensin2 SH2 domain adopts a conserved SH2 fold that mainly consists of five ?-strands flanked by two ?-helices. Most SH2 domains recognize phosphorylated ligands specifically. However, tensin2 SH2 domain was identified to interact with nonphosphorylated ligand (DLC-1) as well as phosphorylated ligand.We determined the solution structure of tensin2 SH2 domain using NMR spectroscopy, and revealed the interactions between tensin2 SH2 domain and its ligands in a phosphotyrosine-independent manner.

SUBMITTER: Dai K

PROVIDER: S-EPMC3134462 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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

Dai Kun K Liao Shanhui S Zhang Jiahai J Zhang Xuecheng X Tu Xiaoming X

PloS one 20110712 7

<h4>Background</h4>Src homology 2 (SH2) domain is a conserved module involved in various biological processes. Tensin family member was reported to be involved in tumor suppression by interacting with DLC-1 (deleted-in-liver-cancer-1) via its SH2 domain. We explore here the important questions that what the structure of tensin2 SH2 domain is, and how it binds to DLC-1, which might reveal a novel binding mode.<h4>Principal findings</h4>Tensin2 SH2 domain adopts a conserved SH2 fold that mainly co ...[more]

PMID: 21765928

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