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| Content Provider | PubMed Central |
|---|---|
| Author | Kahmann, Jan D. Wecking, Diana A. Putter, Vera Lowenhaupt, Ky Kim, Yang-gyun Schmieder, Peter Oschkinat, Hartmut Rich, Alexander Schade, Markus |
| Copyright Year | 2004 |
| Abstract | The N-terminal domain of the vaccinia virus protein E3L (ZαE3L) is essential for full viral pathogenicity in mice. It has sequence similarity to the high-affinity human Z-DNA-binding domains ZαADAR1 and ZαDLM1. Here, we report the solution structure of ZαE3L and the chemical shift map of its interaction surface with Z-DNA. The global structure and the Z-DNA interaction surface of ZαE3L are very similar to the high-affinity Z-DNA-binding domains ZαADAR1 and ZαDLM1. However, the key Z-DNA contacting residue Y48 of ZαE3L adopts a different side chain conformation in unbound ZαE3L, which requires rearrangement for binding to Z-DNA. This difference suggests a molecular basis for the significantly lower in vitro affinity of ZαE3L to Z-DNA compared with its homologues. |
| Related Links | http://dx.doi.org/10.1073/pnas.0308612100 |
| Ending Page | 2717 |
| Page Count | 6 |
| Starting Page | 2712 |
| File Format | |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 9 |
| Volume Number | 101 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2004-03-02 |
| Access Restriction | Open |
| Rights Holder | National Academy of Sciences |
| Subject Keyword | General Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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