Fold of the conserved DTC domain in deltex proteins
Abstract
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.
- Authors:
-
- Toronto
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- FOREIGNINDUSTRY
- OSTI Identifier:
- 1038285
- Resource Type:
- Journal Article
- Journal Name:
- Proteins
- Additional Journal Information:
- Journal Volume: 80; Journal Issue: 5; Journal ID: ISSN 0887-3585
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; CRYSTAL STRUCTURE; LIGASES; PROTEINS
Citation Formats
Obiero, Josiah, Walker, John R, and Dhe-Paganon, Sirano. Fold of the conserved DTC domain in deltex proteins. United States: N. p., 2012.
Web. doi:10.1002/prot.24054.
Obiero, Josiah, Walker, John R, & Dhe-Paganon, Sirano. Fold of the conserved DTC domain in deltex proteins. United States. https://doi.org/10.1002/prot.24054
Obiero, Josiah, Walker, John R, and Dhe-Paganon, Sirano. 2012.
"Fold of the conserved DTC domain in deltex proteins". United States. https://doi.org/10.1002/prot.24054.
@article{osti_1038285,
title = {Fold of the conserved DTC domain in deltex proteins},
author = {Obiero, Josiah and Walker, John R and Dhe-Paganon, Sirano},
abstractNote = {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.},
doi = {10.1002/prot.24054},
url = {https://www.osti.gov/biblio/1038285},
journal = {Proteins},
issn = {0887-3585},
number = 5,
volume = 80,
place = {United States},
year = {Mon Apr 30 00:00:00 EDT 2012},
month = {Mon Apr 30 00:00:00 EDT 2012}
}