MoRFs

Le Molecular Recognition Features (MoRFs) sono piccole (10-70 residui) regioni intrinsecamente disordinate di proteine che subiscono una transizione da disordinate a ordinate in seguito al legame con i loro partner. Le MoRFs sono implicate nelle interazioni proteina-proteina, che servono come passo iniziale nel riconoscimento molecolare. Le MoRF sono disordinate prima del legame con i loro partner, mentre formano una struttura proteica comune dopo l'interazione con i loro partner.

Composizione amminoacidica

La loro composizione di amminoacidi è molto interessante. Sembrano proteine disordinate, ma hanno alcune caratteristiche delle proteine ordinate.

Classificazione

Le MoRF possono essere classificate in 4 categorie in base alla forma che formano una volta legate ai loro partner:

α-MoRFs (quando formano alfa eliche)
β-MoRFs (quando formano Foglietti β)
irregular-MoRFs (quando non si ha alcuna forma)
complex-MoRFs (una combinazione delle categorie sopracitate)

MoRFs Predictors

MoRFPred
ANCHOR Archiviato il 23 ottobre 2009 in Internet Archive.
MoRFchibi SYSTEM
OPAL

Databases

Note

↑ 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 e M. Madan Babu, Classification of intrinsically disordered regions and proteins, in Chem Rev, vol. 114, n. 13, 2014, pp. 6589-631, DOI:10.1021/cr400525m, PMC 4095912, PMID 24773235.
1 2 3 Amrita Mohan, Christopher J. Oldfield, Predrag Radivojac, Vladimir Vacic, Marc S. Cortese, A. Keith Dunker e Vladimir N. Uversky, Analysis of Molecular Recognition Features (MoRFs), in Journal of Molecular Biology, vol. 362, n. 5, 2006, pp. 1043-59, DOI:10.1016/j.jmb.2006.07.087, PMID 16935303.
↑ Disfani FM, Hsu WL, Mizianty MJ, Oldfield CJ, Xue B, Dunker AK, Uversky VN, Kurgan L, MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins, in Bioinformatics, vol. 28, n. 12, 2012, pp. i75–83, DOI:10.1093/bioinformatics/bts209, PMC 3371841, PMID 22689782.
↑ Bálint Mészáros, István Simon e Zsuzsanna Dosztányi, Prediction of protein binding regions in disordered proteins, in PLoS Comput Biol, vol. 5, n. 5, 2009, pp. e1000376, Bibcode:2009PLSCB...5E0376M, DOI:10.1371/journal.pcbi.1000376, PMC 2671142, PMID 19412530.
↑ Nawar Malhis e Joerg Gsponer, Computational Identification of MoRFs in Protein Sequences, in Bioinformatics, vol. 31, n. 11, 2015, pp. 1738-44, DOI:10.1093/bioinformatics/btv060, PMC 4443681, PMID 25637562.
↑ Nawar Malhis, Eric TC Wong, Roy Nassar e Joerg Gsponer, Computational Identification of MoRFs in Protein Sequences Using Hierarchical Application of Bayes Rule, in PLOS ONE, vol. 10, n. 10, 2015, pp. e0141603, Bibcode:2015PLoSO..1041603M, DOI:10.1371/journal.pone.0141603, PMC 4627796, PMID 26517836.
↑ Nawar Malhis, Matthew Jacobson e Jörg Gsponer, MoRFchibi SYSTEM: Software Tools for the Identification of MoRFs in Protein sequences, in Nucleic Acids Research, vol. 44, 2016, pp. gkw409, DOI:10.1093/nar/gkw409, PMID 27174932.
↑ Sharma R, Raicar G, Tsunoda T, Patil A, Sharma A, OPAL: prediction of MoRF regions in intrinsically disordered protein sequence, in Bioinformatics, 2018, DOI:10.1093/bioinformatics/bty032, PMID 29360926.
↑ Foivos Gypas, Georgios N Tsaousis e Stavros J Hamodrakas, mpMoRFsDB: A database of Molecular Recognition Features in Membrane Proteins, in Bioinformatics, vol. 29, n. 19, 2013, pp. 2517-8, DOI:10.1093/bioinformatics/btt427, PMID 23894139.
↑ Erzsébet Fichó, István Reményi e István Simon, MFIB: a repository of protein complexes with mutual folding induced by binding, in Bioinformatics (Oxford, England), vol. 33, n. 22, 15 novembre 2017, pp. 3682-3684, DOI:10.1093/bioinformatics/btx486. URL consultato il 13 aprile 2018.

Portale Biologia: accedi alle voci di Wikipedia che trattano di biologia

[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 e M. Madan Babu, Classification of intrinsically disordered regions and proteins, in Chem Rev, vol. 114, n. 13, 2014, pp. 6589-631, DOI:10.1021/cr400525m, PMC 4095912, PMID 24773235.

[ref2006-2] 1 2 3 Amrita Mohan, Christopher J. Oldfield, Predrag Radivojac, Vladimir Vacic, Marc S. Cortese, A. Keith Dunker e Vladimir N. Uversky, Analysis of Molecular Recognition Features (MoRFs), in Journal of Molecular Biology, vol. 362, n. 5, 2006, pp. 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, MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins, in Bioinformatics, vol. 28, n. 12, 2012, pp. i75–83, DOI:10.1093/bioinformatics/bts209, PMC 3371841, PMID 22689782.

[4] Bálint Mészáros, István Simon e Zsuzsanna Dosztányi, Prediction of protein binding regions in disordered proteins, in PLoS Comput Biol, vol. 5, n. 5, 2009, pp. e1000376, Bibcode:2009PLSCB...5E0376M, DOI:10.1371/journal.pcbi.1000376, PMC 2671142, PMID 19412530.

[5] Nawar Malhis e Joerg Gsponer, Computational Identification of MoRFs in Protein Sequences, in Bioinformatics, vol. 31, n. 11, 2015, pp. 1738-44, DOI:10.1093/bioinformatics/btv060, PMC 4443681, PMID 25637562.

[6] Nawar Malhis, Eric TC Wong, Roy Nassar e Joerg Gsponer, Computational Identification of MoRFs in Protein Sequences Using Hierarchical Application of Bayes Rule, in PLOS ONE, vol. 10, n. 10, 2015, pp. e0141603, Bibcode:2015PLoSO..1041603M, DOI:10.1371/journal.pone.0141603, PMC 4627796, PMID 26517836.

[MCS2016-7] Nawar Malhis, Matthew Jacobson e Jörg Gsponer, MoRFchibi SYSTEM: Software Tools for the Identification of MoRFs in Protein sequences, in Nucleic Acids Research, vol. 44, 2016, pp. gkw409, DOI:10.1093/nar/gkw409, PMID 27174932.

[8] Sharma R, Raicar G, Tsunoda T, Patil A, Sharma A, OPAL: prediction of MoRF regions in intrinsically disordered protein sequence, in Bioinformatics, 2018, DOI:10.1093/bioinformatics/bty032, PMID 29360926.

[9] Foivos Gypas, Georgios N Tsaousis e Stavros J Hamodrakas, mpMoRFsDB: A database of Molecular Recognition Features in Membrane Proteins, in Bioinformatics, vol. 29, n. 19, 2013, pp. 2517-8, DOI:10.1093/bioinformatics/btt427, PMID 23894139.

[10] Erzsébet Fichó, István Reményi e István Simon, MFIB: a repository of protein complexes with mutual folding induced by binding, in Bioinformatics (Oxford, England), vol. 33, n. 22, 15 novembre 2017, pp. 3682-3684, DOI:10.1093/bioinformatics/btx486. URL consultato il 13 aprile 2018.