1TTN

Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells

1TTN の概要

• エントリーDOI: 10.2210/pdb1ttn/pdb
• NMR情報: BMRB: 6609
• 分子名称: dendritic cell-derived ubiquitin-like protein (1 entity in total)
• 機能のキーワード: ubiquitin-like domain, dc-ubp, solution structure, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q8WUN7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12180.95

構造登録者

Hu, H.Y. (登録日: 2004-06-23, 公開日: 2005-07-05, 最終更新日: 2024-05-29)

主引用文献

Gao, Y.G.,Song, A.X.,Shi, Y.H.,Chang, Y.G.,Liu, S.X.,Yu, Y.Z.,Cao, X.T.,Lin, D.H.,Hu, H.Y.
Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells
Protein Sci., 14:2044-2050, 2005

PubMed Abstract: The previously identified dendritic cell-derived ubiquitin-like protein (DC-UbP) was implicated in cellular differentiation and apoptosis. Sequence alignment suggested that it contains a ubiquitin-like (UbL) domain in the C terminus. Here, we present the solution NMR structure and backbone dynamics of the UbL domain of DC-UbP. The overall structure of the domain is very similar to that of Ub despite low similarity (<30%) in amino-acid sequence. One distinct feature of the domain structure is its highly positively charged surface that is different from the corresponding surfaces of the well-known UbL modifiers, Ub, NEDD8, and SUMO-1. The key amino-acid residues responsible for guiding polyubiquitinated proteins to proteasome degradation in Ub are not conserved in the UbL domain. This implies that the UbL domain of DC-UbP may have its own specific interaction partners with other yet unknown cellular functions related to the Ub pathway.

PubMed: 15987890
DOI: 10.1110/ps.051455505

実験手法

SOLUTION NMR