Molecular recognition feature

Molecular recognition features (MoRFs) are small (10-70 residues) intrinsically disordered regions in proteins that undergo a disorder-to-order transition upon binding to their partners. MoRFs are implicated in protein-protein interactions, which serve as the initial step in molecular recognition. MoRFs are disordered prior binding to their partners, whereas they form a common 3D structure after interacting with their partners.[1][2]

Amino acid composition

Their amino acid composition is very interesting. They look like disordered proteins, but they have some characteristics of ordered proteins.[2]

Categorization

MoRFs can be separated in 4 categories according to the shape they form once bound to their partners.[2]

The categories are:

  • α-MoRFs (when they form alpha-helixes)
  • β-MoRFs (when they form beta-sheets)
  • irregular-MoRFs (when they don't form any shape)
  • complex-MoRFs (combination of the above categories)

MoRFs Predictors

MoRFPred[3] ANCHOR[4] MoRFchibi SYSTEM[5][6][7] OPAL[8]

Databases

mpMoRFsDB[9]

Mutual Folding Induced by Binding (MFIB) database[10]

References

  1. ↑ Robin van der Lee; Marija Buljan; Benjamin Lang; Robert J. Weatheritt; Gary W. Daughdrill; A. Keith Dunker; Monika Fuxreiter; Julian Gough; Joerg Gsponer; David T. Jones; Philip M. Kim; Richard W. Kriwacki; Christopher J. Oldfield; Rohit V. Pappu; Peter Tompa; Vladimir N. Uversky; Peter E. Wright; M. Madan Babu (2014). "Classification of intrinsically disordered regions and proteins". Chem Rev. 114 (13): 6589–631. doi:10.1021/cr400525m. PMC 4095912. PMID 24773235.
  2. 1 2 3 Amrita Mohan; Christopher J. Oldfield; Predrag Radivojac; Vladimir Vacic; Marc S. Cortese; A. Keith Dunker; Vladimir N. Uversky (2006). "Analysis of Molecular Recognition Features (MoRFs)". Journal of Molecular Biology. 362 (5): 1043–59. doi:10.1016/j.jmb.2006.07.087. PMID 16935303.
  3. ↑ Disfani FM, Hsu WL, Mizianty MJ, Oldfield CJ, Xue B, Dunker AK, Uversky VN, Kurgan L (2012). "MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins". Bioinformatics. 28 (12): i75–83. doi:10.1093/bioinformatics/bts209. PMC 3371841. PMID 22689782.
  4. ↑ Bálint Mészáros; István Simon; Zsuzsanna Dosztányi (2009). "Prediction of protein binding regions in disordered proteins". PLoS Comput Biol. 5 (5): e1000376. Bibcode:2009PLSCB...5E0376M. doi:10.1371/journal.pcbi.1000376. PMC 2671142. PMID 19412530.
  5. ↑ Nawar Malhis & Joerg Gsponer (2015). "Computational Identification of MoRFs in Protein Sequences". Bioinformatics. 31 (11): 1738–44. doi:10.1093/bioinformatics/btv060. PMC 4443681. PMID 25637562.
  6. ↑ Nawar Malhis; Eric TC Wong; Roy Nassar; Joerg Gsponer (2015). "Computational Identification of MoRFs in Protein Sequences Using Hierarchical Application of Bayes Rule". PLOS ONE. 10 (10): e0141603. Bibcode:2015PLoSO..1041603M. doi:10.1371/journal.pone.0141603. PMC 4627796. PMID 26517836.
  7. ↑ Nawar Malhis; Matthew Jacobson; Jörg Gsponer (2016). "MoRFchibi SYSTEM: Software Tools for the Identification of MoRFs in Protein sequences". Nucleic Acids Research. 44: gkw409. doi:10.1093/nar/gkw409. PMID 27174932.
  8. ↑ Sharma R, Raicar G, Tsunoda T, Patil A, Sharma A (2018). "OPAL: prediction of MoRF regions in intrinsically disordered protein sequence". Bioinformatics. doi:10.1093/bioinformatics/bty032. PMID 29360926.
  9. ↑ Foivos Gypas; Georgios N Tsaousis; Stavros J Hamodrakas (2013). "mpMoRFsDB: A database of Molecular Recognition Features in Membrane Proteins". Bioinformatics. 29 (19): 2517–8. doi:10.1093/bioinformatics/btt427. PMID 23894139.
  10. ↑ Erzsébet Fichó; István Reményi; István Simon; Bálint Mészáros (2017). "MFIB: a repository of protein complexes with mutual folding induced by binding". Bioinformatics. doi:10.1093/bioinformatics/btx486.
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