ArticleNucleic acids research2017
Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- Human SRP Subunits Coordinate Protein Targeting and mRNA Quality Control.bioRxiv : the preprint server for biology · 2026Article
- A De Novo Splicing Mutation of SRP72 in Bone Marrow Failure Syndrome Type 1: Case Report and Review of the Literature.Molecular genetics & genomic medicine · 2026Review
- All-at-once RNA folding with 3D motif prediction framed by evolutionary information.Nature methods · 2025Article
- Solution structure determination and biophysical characterization studies of 7SK RNP and 7SL SRP RNAs.RNA (New York, N.Y.) · 2025Article
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- Article
- Development of Stimuli-Responsive Polymeric Nanomedicines in Hypoxic Tumors and Their Therapeutic Promise in Oral Cancer.Polymers · 2025Review
- Cryo-EM structure of SRP68/72 reveals an extended dimerization domain with RNA-binding activity.Nucleic acids research · 2024Article
- Profiling non-coding RNA levels with clinical classifiers in pediatric Crohn's disease.BMC medical genomics · 2021Article
- Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle.Cell reports · 2021Article
- SRPassing Co-translational Targeting: The Role of the Signal Recognition Particle in Protein Targeting and mRNA Protection.International journal of molecular sciences · 2021Review
- Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation.Communications biology · 2021Article
- Article
- New progress in the study of germline susceptibility genes of myeloid neoplasms.Oncology letters · 2021Review
- Structural basis of Naa20 activity towards a canonical NatB substrate.Communications biology · 2021Article
- Noncanonical Functions and Cellular Dynamics of the Mammalian Signal Recognition Particle Components.Frontiers in molecular biosciences · 2021Review
- WGCNA Identification of Genes and Pathways Involved in the Pathogenesis of Postmenopausal Osteoporosis.International journal of general medicine · 2021Article
- Integrative Network Biology Framework Elucidates Molecular Mechanisms of SARS-CoV-2 Pathogenesis.SSRN · 2020Article
- Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions.Nucleic acids research · 2019Article
- Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex.Science (New York, N.Y.) · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Co-translational protein targeting and membrane protein insertion is a fundamental process and depends on the signal recognition particle (SRP). In mammals, SRP is composed of the SRP RNA crucial for SRP assembly and function and six proteins. The two largest proteins SRP68 and SRP72 form a heterodimer and bind to a regulatory site of the SRP RNA. Despite their essential roles in the SRP pathway, structural information has been available only for the SRP68 RNA-binding domain (RBD). Here we present the crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP. The SRP72-PBD is a tetratricopeptide repeat, which binds an extended linear motif of SRP68 with high affinity. The SRP72-RBD is a flexible peptide crawling along the 5e- and 5f-loops of SRP RNA. A conserved tryptophan inserts into the 5e-loop forming a novel type of RNA kink-turn stabilized by a potassium ion, which we define as K
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.