ArticlePloS one2011
Solution structure of LC4 transmembrane segment of CCR5.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Unique E2-binding specificity of artificial RING fingers in cancer cells.Scientific reports · 2024Article
- Artificial RING finger reveals unique auto-ubiquitination with E2 specificity.Protein science : a publication of the Protein Society · 2023Article
- Solution structure of the zinc finger domain of human RNF144A ubiquitin ligase.Protein science : a publication of the Protein Society · 2020Article
- Zinc finger domain of the human DTX protein adopts a unique RING fold.Protein science : a publication of the Protein Society · 2019Article
- Unique RING finger structure from the human HRD1 protein.Protein science : a publication of the Protein Society · 2019Article
- Unique auto-ubiquitination activities of artificial RING fingers in cancer cells.Protein science : a publication of the Protein Society · 2018Article
- Solution structure of the PHD finger from the human KIAA1045 protein.Protein science : a publication of the Protein Society · 2018Article
- In Silico Studies Targeting G-protein Coupled Receptors for Drug Research Against Parkinson's Disease.Current neuropharmacology · 2018Article
- The unique N-terminal zinc finger of synaptotagmin-like protein 4 reveals FYVE structure.Protein science : a publication of the Protein Society · 2017Article
- The zinc finger domain of RING finger protein 141 reveals a unique RING fold.Protein science : a publication of the Protein Society · 2017Article
- Structural model of ubiquitin transfer onto an artificial RING finger as an E3 ligase.Scientific reports · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CC-chemokine receptor 5 (CCR5) is a specific co-receptor allowing the entry of human immunodeficiency virus type 1 (HIV-1). The LC4 region in CCR5 is required for HIV-1 entry into the cells. In this study, the solution structure of LC4 in SDS micelles was elucidated by using standard 1H two-dimensional NMR spectroscopy, circular dichroism, and fluorescence quenching. The LC4 structure adopts two helical structures, whereas the C-terminal part remains unstructured. The positions in which LC4 binds to the HIV-1 inhibitory peptide LC5 were determined by docking calculations in addition to NMR data. The poses showed the importance of the hydrophobic interface of the assembled structures. The solution structure of LC4 elucidated in the present work provides a structural basis for further studies on the HIV-1 inhibitory function of the LC4 region.
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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.