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Title: 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:
; ;  [1]
  1. (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
Resource Relation:
Journal Name: Proteins; Journal Volume: 80; Journal Issue: 5
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. doi: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. doi: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},
journal = {Proteins},
number = 5,
volume = 80,
place = {United States},
year = 2012,
month = 4
}
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