ArticleMolecular membrane biology2013
Impact of histidine residues on the transmembrane helices of viroporins.
Article in Molecular membrane biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A structural bioinformatics framework for prioritizing pH-sensitive proteins from 3D structural features.BMC bioinformatics · 2026Article
- Comparative Genomics of Viral Genomes and Identification of Three Novel Viroporin-Like Superfamilies.Microbial physiology · 2026Article
- Searching for genes determining the APR phenotype in rye.BMC plant biology · 2025Article
- MARC, a novel modular chimeric antigen receptor, improves T cell-based cancer immunotherapies by preventing early T cell exhaustion and enhancing persistence.Journal for immunotherapy of cancer · 2025Article
- Oligomeric assembly of the C-terminal and transmembrane region of SARS-CoV-2 nsp3.Journal of virology · 2024Article
- Variations in exons 11 and 12 of the multi-pest resistance wheat geneFrontiers in plant science · 2022Article
- Relating structure and function of viral membrane-spanning miniproteins.Current opinion in virology · 2015Review
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
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Authors and funding
4 authors.
Funding
Abstract
Abstract The role of histidine in channel-forming transmembrane (TM) helices was investigated by comparing the TM helices from Virus protein 'u' (Vpu) and the M2 proton channel. Both proteins are members of the viroporin family of small membrane proteins that exhibit ion channel activity, and have a single TM helix that is capable of forming oligomers. The TM helices from both proteins have a conserved tryptophan towards the C-terminus. Previously, alanine 18 of Vpu was mutated to histidine in order to artificially introduce the same HXXXW motif that is central to the proton channel activity of M2. Interestingly, the mutated Vpu TM resulted in an increase in helix tilt angle of 11° in lipid bilayers compared to the wild-type Vpu TM. Here, we find the reverse, when histidine 37 of the HXXXW motif in M2 was mutated to alanine, it decreased the helix tilt by 10° from that of wild-type M2. The tilt change is independent of both the helix length and the presence of tryptophan. In addition, compared to wild-type M2, the H37A mutant displayed lowered sensitivity to proton concentration. We also found that the solvent accessibility of histidine-containing M2 is greater than without histidine. This suggests that the TM helix may increase the solvent exposure by changing its tilt angle in order to accommodate a polar/charged residue within the hydrophobic membrane region. The comparative results of M2, Vpu and their mutants demonstrated the significance of histidine in a transmembrane helix and the remarkable plasticity of the function and structure of ion channels stemming from changes at a single amino acid site.
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