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8J6M

SIDT1 protein

Summary for 8J6M
Entry DOI10.2210/pdb8j6m/pdb
EMDB information36008
DescriptorGreen fluorescent protein,SID1 transmembrane family member 1, CHOLESTEROL, ZINC ION, ... (6 entities in total)
Functional Keywordstransport t1, transcription
Biological sourceAequorea victoria
More
Total number of polymer chains2
Total formula weight251901.31
Authors
Zhang, J.T.,Jiang, D.H. (deposition date: 2023-04-26, release date: 2024-05-01, Last modification date: 2024-10-16)
Primary citationZhang, J.,Zhan, C.,Fan, J.,Wu, D.,Zhang, R.,Wu, D.,Chen, X.,Lu, Y.,Li, M.,Lin, M.,Gong, J.,Jiang, D.
Structural insights into double-stranded RNA recognition and transport by SID-1.
Nat.Struct.Mol.Biol., 31:1095-1104, 2024
Cited by
PubMed Abstract: RNA uptake by cells is critical for RNA-mediated gene interference (RNAi) and RNA-based therapeutics. In Caenorhabditis elegans, RNAi is systemic as a result of SID-1-mediated double-stranded RNA (dsRNA) across cells. Despite the functional importance, the underlying mechanisms of dsRNA internalization by SID-1 remain elusive. Here we describe cryogenic electron microscopy structures of SID-1, SID-1-dsRNA complex and human SID-1 homologs SIDT1 and SIDT2, elucidating the structural basis of dsRNA recognition and import by SID-1. The homodimeric SID-1 homologs share conserved architecture, but only SID-1 possesses the molecular determinants within its extracellular domains for distinguishing dsRNA from single-stranded RNA and DNA. We show that the removal of the long intracellular loop between transmembrane helix 1 and 2 attenuates dsRNA uptake and systemic RNAi in vivo, suggesting a possible endocytic mechanism of SID-1-mediated dsRNA internalization. Our study provides mechanistic insights into dsRNA internalization by SID-1, which may facilitate the development of dsRNA applications based on SID-1.
PubMed: 38664565
DOI: 10.1038/s41594-024-01276-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.77 Å)
Structure validation

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