Ontology highlight
ABSTRACT:
SUBMITTER: Bomar MG
PROVIDER: S-EPMC1808033 | biostudies-literature | 2007 Mar
REPOSITORIES: biostudies-literature
Bomar Martha G MG Pai Ming-Tao MT Tzeng Shiou-Ru SR Li Shawn Shun-Cheng SS Zhou Pei P
EMBO reports 20070216 3
The ubiquitin-binding zinc finger (UBZ) domain of human DNA Y-family polymerase (pol) eta is important in the recruitment of the polymerase to the stalled replication machinery in translesion synthesis. Here, we report the solution structure of the pol eta UBZ domain and its interaction with ubiquitin. We show that the UBZ domain adopts a classical C(2)H(2) zinc-finger structure characterized by a betabetaalpha fold. Nuclear magnetic resonance titration maps the binding interfaces between UBZ an ...[more]