Structural highlights
Publication Abstract from PubMed
Human Deltex 3-like (DTX3L) is a member of the Deltex family of proteins. Initially identified as a B-lymphoma and BAL-associated protein, DTX3L is an E3 ligase that regulates subcellular localization of its partner protein, BAL, by a dynamic nucleocytoplasmic trafficking mechanism. Unlike other members of the Deltex family of proteins, DTX3L lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex proteins, and instead contains other unique N-terminal domains. The C-terminal domains are, however, homologous with other members of the Deltex family of proteins; these include a RING domain and a previously unidentified C-terminal domain. In this study, we report the high-resolution crystal structure of this previously uncharacterized C-terminal domain of human DTX3L, which we term the Deltex C-terminal domain.
Fold of the conserved DTC domain in Deltex proteins.,Obiero J, Walker JR, Dhe-Paganon S Proteins. 2012 May;80(5):1495-9. doi: 10.1002/prot.24054. Epub 2012 Mar 13. PMID:22411408[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Obiero J, Walker JR, Dhe-Paganon S. Fold of the conserved DTC domain in Deltex proteins. Proteins. 2012 May;80(5):1495-9. doi: 10.1002/prot.24054. Epub 2012 Mar 13. PMID:22411408 doi:http://dx.doi.org/10.1002/prot.24054