Sequence variants in the 3'-->5' deoxyribonuclease TREX2: identification in a genetic screen and effects on catalysis by the recombinant proteins.
نویسندگان
چکیده
Fred W. Perrino*, Anna Krol, Scott Harvey, S. Lilly Zheng, David A. Horita, Thomas Hollis, Deborah A. Meyers, William B. Isaacs, Jianfeng Xu Department of Biochemistry, Wake Forest University Health Sciences, Winston-Salem, NC 27157, USA Center for Human Genomics, Wake Forest University Health Sciences, Winston-Salem, NC 27157, USA Brady Urological Institute Research Laboratories, Johns Hopkins School of Medicine, Baltimore, MD 21287, USA
منابع مشابه
The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis.
The 3' --> 5'-exonucleases process DNA ends in many DNA repair pathways of human cells. Determination of the human TREX2 structure is the first of a dimeric 3'-deoxyribonuclease and indicates how this highly efficient nonprocessive enzyme removes nucleotides at DNA 3' termini. Symmetry in the TREX2 dimer positions the active sites at opposite outer edges providing open access for the DNA. Adjac...
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ورودعنوان ژورنال:
- Advances in enzyme regulation
دوره 44 شماره
صفحات -
تاریخ انتشار 2004