The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes. Issue Volume 49:Issue D1(2021) (29th October 2020)

• Record Type: Journal Article
• Authors: Csizmadia, Georgina; Erdős, Gábor; Tordai, Hedvig; Padányi, Rita; Tosatto, Silvio; Dosztányi, Zsuzsanna; Hegedűs, Tamás
• Is Part Of: Nucleic acids research. Volume 49:Issue D1(2021)
• Page Start: D355
• Page End: D360
• Publication Date: 2020-10-29
• Subjects: Nucleic acids -- Periodicals; Molecular biology -- Periodicals; 572.805
• DOI: 10.1093/nar/gkaa954
• Languages: English
• ISSNs: 0305-1048

Abstract

Abstract: Protein and lipid membrane interactions play fundamental roles in a large number of cellular processes (e.g. signalling, vesicle trafficking, or viral invasion). A growing number of examples indicate that such interactions can also rely on intrinsically disordered protein regions (IDRs), which can form specific reversible interactions not only with proteins but also with lipids. We named IDRs involved in such membrane lipid-induced disorder-to-order transition as MemMoRFs, in an analogy to IDRs exhibiting disorder-to-order transition upon interaction with protein partners termed Molecular Recognition Features (MoRFs). Currently, both the experimental detection and computational characterization of MemMoRFs are challenging, and information about these regions are scattered in the literature. To facilitate the related investigations we generated a comprehensive database of experimentally validated MemMoRFs based on manual curation of literature and structural data. To characterize the dynamics of MemMoRFs, secondary structure propensity and flexibility calculated from nuclear magnetic resonance chemical shifts were incorporated into the database. These data were supplemented by inclusion of sentences from papers, functional data and disease-related information. The MemMoRF database can be accessed via a user-friendly interface at https://memmorf.hegelab.org, potentially providing a central resource for the characterization of disordered regions in transmembrane and membrane-associated proteins.