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http://purl.uniprot.org/citations/21765928http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21765928http://www.w3.org/2000/01/rdf-schema#comment"

Background

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.

Principal findings

Tensin2 SH2 domain adopts a conserved SH2 fold that mainly consists of five β-strands flanked by two α-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.

Conclusions

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."xsd:string
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http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/author"Zhang J."xsd:string
http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/author"Tu X."xsd:string
http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/author"Liao S."xsd:string
http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/author"Dai K."xsd:string
http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/name"PLoS One"xsd:string
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http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/title"Solution structure of tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1."xsd:string
http://purl.uniprot.org/citations/21765928http://purl.uniprot.org/core/volume"6"xsd:string
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