Structural analysis of the catalytic domain of Artemis endonuclease/SNM1C reveals distinct structural features.

ABSTRACT: The endonuclease Artemis is responsible for opening DNA hairpins during V(D)J recombination and for processing a subset of pathological DNA double-strand breaks. Artemis is an attractive target for the development of therapeutics to manage various B cell and T cell tumors, because failure to open DNA hairpins and accumulation of chromosomal breaks may reduce the proliferation and viability of pre-T and pre-B cell derivatives. However, structure-based drug discovery of specific Artemis inhibitors has been hampered by a lack of crystal structures. Here, we report the structure of the catalytic domain of recombinant human Artemis. The catalytic domain displayed a polypeptide fold similar overall to those of other members in the DNA cross-link repair gene SNM1 family and in mRNA 3'-end-process

SUBMITTER: Karim MF 

PROVIDER: S-EPMC7458816 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature