Structural highlights
Function
[TENC1_HUMAN] Regulates cell motility and proliferation. May have phosphatase activity. Reduces AKT1 phosphorylation. Lowers AKT1 kinase activity and interferes with AKT1 signaling.[1]
Publication Abstract from PubMed
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 beta-strands flanked by two alpha-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.
Solution structure of Tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1.,Dai K, Liao S, Zhang J, Zhang X, Tu X PLoS One. 2011;6(7):e21965. Epub 2011 Jul 12. PMID:21765928[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hafizi S, Ibraimi F, Dahlback B. C1-TEN is a negative regulator of the Akt/PKB signal transduction pathway and inhibits cell survival, proliferation, and migration. FASEB J. 2005 Jun;19(8):971-3. Epub 2005 Apr 7. PMID:15817639 doi:http://dx.doi.org/10.1096/fj.04-2532fje
- ↑ Dai K, Liao S, Zhang J, Zhang X, Tu X. Solution structure of Tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1. PLoS One. 2011;6(7):e21965. Epub 2011 Jul 12. PMID:21765928 doi:10.1371/journal.pone.0021965
