title: Solution structure of tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1.
abstract: 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.
  
  
  RESULTS
  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.
authors.affiliation: Hefei 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.
authors.forename: Kun
authors.initials: K
authors.lastname: Dai
authors.forename: Shanhui
authors.initials: S
authors.lastname: Liao
authors.forename: Jiahai
authors.initials: J
authors.lastname: Zhang
authors.forename: Xuecheng
authors.initials: X
authors.lastname: Zhang
authors.forename: Xiaoming
authors.initials: X
authors.lastname: Tu
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006801:Humans; D007700:Kinetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008840:Microfilament Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D012996:Solutions; D013329:Structure-Activity Relationship; D020349:Surface Plasmon Resonance; D000070876:Tensins; D025521:Tumor Suppressor Proteins / Q000737:chemistry / Q000378:metabolism*; D018909:src Homology Domains
chemical_list: D008024:Ligands; D008840:Microfilament Proteins; D010455:Peptides; D012996:Solutions; D000070876:Tensins; D025521:Tumor Suppressor Proteins; D019000:Phosphotyrosine; C452816:TNS2 protein, human; D010744:Phosphoric Monoester Hydrolases