2MBQ

K11-linked Diubiquitin average solution structure at pH 6.8, 150 mM NaCl

2MBQ の概要

• エントリーDOI: 10.2210/pdb2mbq/pdb
• 関連するPDBエントリー: 2MBO
• NMR情報: BMRB: 19412
• 分子名称: Ubiquitin (1 entity in total)
• 機能のキーワード: diubiquitin, k11, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Ubiquitin: Cytoplasm (By similarity): P0CG48
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17153.66

構造登録者

Castaneda, C.A.,Fushman, D. (登録日: 2013-08-03, 公開日: 2013-09-04, 最終更新日: 2024-05-15)

主引用文献

Castaneda, C.A.,Kashyap, T.R.,Nakasone, M.A.,Krueger, S.,Fushman, D.
Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains.
Structure, 21:1168-1181, 2013

PubMed Abstract: K11-linked polyubiquitin chains play important signaling and regulatory roles in both degradative and nonproteolytic pathways in eukaryotes. To understand the structural basis of how these chains are recognized and distinguished from other polyubiquitins, we determined solution structures of K11-linked diubiquitin (K11-Ub2) in the absence and presence of salt. These structures reveal that K11-Ub2 adopts conformations distinct from those of K48-linked or K63-linked chains. Importantly, our solution NMR and SANS data are inconsistent with published crystal structures of K11-Ub2. We found that increasing salt concentration compacts K11-Ub2 and strengthens interactions between the two Ub units. Binding studies indicate that K11-Ub2 interacts with ubiquitin-receptor proteins from both proteasomal and nonproteasomal pathways but with intermediate affinity and different binding modes than either K48-linked or K63-linked diubiquitin. Our data support the hypothesis that polyubiquitin chains of different linkages possess unique conformational and dynamical properties, allowing them to be recognized differently by downstream receptor proteins.

PubMed: 23823328
DOI: 10.1016/j.str.2013.04.029

実験手法

SOLUTION NMR