ArticleProtein science : a publication of the Protein Society2018
Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- The role of hypoxic microenvironment in autoimmune diseases.Frontiers in immunology · 2024Review
- Unraveling the complex genetics of neural tube defects: From biological models to human genomics and back.Genesis (New York, N.Y. : 2000) · 2021Review
- FKBP8 variants are risk factors for spina bifida.Human molecular genetics · 2020Article
- NMR- and MD simulation-based structural characterization of the membrane-associating FATC domain of ataxia telangiectasia mutated.The Journal of biological chemistry · 2019Article
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3 authors.
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Abstract
Increased efforts have been undertaken to better understand the formation of signaling complexes at cellular membranes. Since the preparation of proteins containing a transmembrane domain or a prenylation motif is generally challenging an alternative membrane anchoring unit that is easy to attach, water-soluble and binds to different membrane mimetics would find broad application. The 33-residue long FATC domain of yeast TOR1 (y1fatc) fulfills these criteria and binds to neutral and negatively charged micelles, bicelles, and liposomes. As a case study, we fused it to the FKBP506-binding region of the protein FKBP38 (FKBP38-BD) and used
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