8V38

Structure of the human systemic RNAi defective transmembrane protein 1 (hSIDT1)

8V38 の概要

• エントリーDOI: 10.2210/pdb8v38/pdb
• EMDBエントリー: 42943
• 分子名称: SID1 transmembrane family member 1,RNA-directed RNA polymerase L (1 entity in total)
• 機能のキーワード: rna interference, transmembrane protein, cholesterol or dsrna uptake family., membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 248196.28

構造登録者

Navratna, V.,Kumar, A.,Rana, J.K.,Mosalaganti, S. (登録日: 2023-11-27, 公開日: 2024-06-26, 最終更新日: 2026-02-18)

主引用文献

Navratna, V.,Kumar, A.,Rana, J.K.,Mosalaganti, S.
Structure of the human systemic RNAi defective transmembrane protein 1 (hSIDT1) reveals the conformational flexibility of its lipid binding domain.
Life Sci Alliance, 7:-, 2024

PubMed Abstract: In , inter-cellular transport of the small non-coding RNA causing systemic RNAi is mediated by the transmembrane protein SID1, encoded by the gene in the systemic RNAi defective () loci. SID1 shares structural and sequence similarity with cholesterol uptake protein 1 (CHUP1) and is classified as a member of the ChUP family. Although systemic RNAi is not an evolutionarily conserved process, the gene products are found across the animal kingdom, suggesting the existence of other novel gene regulatory mechanisms mediated by small non-coding RNAs. Human homologs of gene products-hSIDT1 and hSIDT2-mediate contact-dependent lipophilic small non-coding dsRNA transport. Here, we report the structure of recombinant human SIDT1. We find that the extra-cytosolic domain of hSIDT1 adopts a double jelly roll fold, and the transmembrane domain exists as two modules-a flexible lipid binding domain and a rigid transmembrane domain core. Our structural analyses provide insights into the inherent conformational dynamics within the lipid binding domain in ChUP family members.

PubMed: 38925866
DOI: 10.26508/lsa.202402624

実験手法

ELECTRON MICROSCOPY (3.5 Å)