title: 1H, 15N and 13C chemical shift assignments of the SH2 domain of human tensin2 (TENC1).
abstract: Tensin is an important cytoplasmic phosphoprotein localized to integrin-mediated focal adhesion. It links actin cytoskeleton to extracellular matrix through its N-terminal actin-binding domain and C-terminal phosphotyrosine-binding domain. Studies of knockout mice revealed the critical roles of tensin in skeletal muscle regeneration, renal function and regulation of cell migration. The SH2 domain of tensin interacts with various tyrosine-phosphorylated proteins thus functions as a platform for dis/assembly of signaling molecules. It has also been implicated in recruiting a tumor supperssor protein DLC1 (deleted in live cancer 1) to the focal adhesion, which is required for oncogenic inhibition effect of DLC1 in a phosphotyrosine-independent manner. Here, we report complete chemical shift assignments of the SH2 domain of human tensin2 determined by triple resonance experiments. The resonance assignments serve as a basis for our further functional studies and structure determination by NMR spectroscopy. (BMRB deposits with accession number 16472).
authors.affiliation: Division of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
authors.forename: Lihong
authors.initials: L
authors.lastname: Chen
authors.forename: Changdong
authors.initials: C
authors.lastname: Liu
authors.forename: Feng
authors.initials: F
authors.lastname: Rui
authors.forename: Guang
authors.initials: G
authors.lastname: Zhu
mesh_terms: D006801:Humans; D007554:Isotopes; D008840:Microfilament Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D000070876:Tensins; D018909:src Homology Domains
chemical_list: D007554:Isotopes; D008840:Microfilament Proteins; D011994:Recombinant Proteins; D000070876:Tensins; C452816:TNS2 protein, human; D010744:Phosphoric Monoester Hydrolases