Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-12

AUTHORS

Thorsten Dieckmann, Elizabeth S. Withers-Ward, Mark A. Jarosinski, Chuan-Fa Liu, Irvin S. Y. Chen, Juli Feigon

ABSTRACT

The HIV-1 protein Vpr is critical for a number of viral functions including a unique ability to arrest T-cells at a G2/M checkpoint and induce subsequent apoptosis. It has been shown to interact specifically with the second UBA (ubiquitin associated) domain found in the DNA repair protein HHR23A, a highly evolutionarily conserved protein. This domain is a commonly occurring sequence motif in some members of the ubiquitination pathway, UV excision repair proteins, and certain protein kinases. The three dimensional structure of the UBA domain, determined by NMR spectroscopy, is presented. The protein domain forms a compact three-helix bundle. One side of the protein has a hydrophobic surface that is the most likely Vpr target site. More... »

PAGES

nsb1298_1042

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/4220

DOI

http://dx.doi.org/10.1038/4220

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1049242268

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9846873


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