5O0N

Deglycosylated Nogo Receptor with native disulfide structure 4

5O0N の概要

• エントリーDOI: 10.2210/pdb5o0n/pdb
• 分子名称: Reticulon-4 receptor, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: nervous system, signaling, leucine-rich repeat domain, disulfide structure, signaling protein
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cell membrane ; Lipid-anchor, GPI-anchor : Q99PI8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38328.16

構造登録者

Pronker, M.F.,Tas, R.P.,Vlieg, H.C.,Janssen, B.J.C. (登録日: 2017-05-16, 公開日: 2017-10-18, 最終更新日: 2024-10-16)

主引用文献

Pronker, M.F.,Tas, R.P.,Vlieg, H.C.,Janssen, B.J.C.
Nogo Receptor crystal structures with a native disulfide pattern suggest a novel mode of self-interaction.
Acta Crystallogr D Struct Biol, 73:860-876, 2017

PubMed Abstract: The Nogo Receptor (NgR) is a glycophosphatidylinositol-anchored cell-surface protein and is a receptor for three myelin-associated inhibitors of regeneration: myelin-associated glycoprotein, Nogo66 and oligodendrocyte myelin glycoprotein. In combination with different co-receptors, NgR mediates signalling that reduces neuronal plasticity. The available structures of the NgR ligand-binding leucine-rich repeat (LRR) domain have an artificial disulfide pattern owing to truncated C-terminal construct boundaries. NgR has previously been shown to self-associate via its LRR domain, but the structural basis of this interaction remains elusive. Here, crystal structures of the NgR LRR with a longer C-terminal segment and a native disulfide pattern are presented. An additional C-terminal loop proximal to the C-terminal LRR cap is stabilized by two newly formed disulfide bonds, but is otherwise mostly unstructured in the absence of any stabilizing interactions. NgR crystallized in six unique crystal forms, three of which share a crystal-packing interface. NgR crystal-packing interfaces from all eight unique crystal forms are compared in order to explore how NgR could self-interact on the neuronal plasma membrane.

PubMed: 29095159
DOI: 10.1107/S2059798317013791

実験手法

X-RAY DIFFRACTION (2.5 Å)