@article{open1897,
          volume = {84},
          number = {10},
           month = {October},
          author = {Anu Priyanka and Vipul Solanki and Raman Parkesh and Krishan Gopal Thakur},
            note = {Open Access},
           title = {Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture.},
       publisher = {Wiley},
            year = {2016},
         journal = {Proteins},
           pages = {1558--63},
        keywords = {Human SIRT7; histone deacetylase; maltose binding protein; peptide mass fingerprinting; sirtuins; x-ray crystallography},
             url = {http://crdd.osdd.net/open/1897/},
        abstract = {Human SIRT7 is an NAD(+) dependent deacetylase, which belongs to sirtuin family of proteins. SIRT7, like other sirtuins has conserved catalytic domain and is flanked by N- and C-terminal domains reported to play vital functional roles. Here, we report the crystal structure of the N-terminal domain of human SIRT7 (SIRT7(NTD) ) at 2.3 {\rA} resolution as MBP-SIRT7(NTD) fusion protein. SIRT7(NTD) adopts three-helical domain architecture and comparative structural analyses suggest similarities to some DNA binding motifs and transcription regulators. We also report here the importance of N- and C-terminal domains in soluble expression of SIRT7. Proteins 2016; 84:1558-1563. {\copyright} 2016 Wiley Periodicals, Inc.}
}