Low-resolution description of the conformational space for intrinsically disordered proteins.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
09 11 2022
Historique:
received: 01 05 2022
accepted: 29 09 2022
entrez: 9 11 2022
pubmed: 10 11 2022
medline: 15 11 2022
Statut: epublish

Résumé

Intrinsically disordered proteins (IDP) are at the center of numerous biological processes, and attract consequently extreme interest in structural biology. Numerous approaches have been developed for generating sets of IDP conformations verifying a given set of experimental measurements. We propose here to perform a systematic enumeration of protein conformations, carried out using the TAiBP approach based on distance geometry. This enumeration was performed on two proteins, Sic1 and pSic1, corresponding to unphosphorylated and phosphorylated states of an IDP. The relative populations of the obtained conformations were then obtained by fitting SAXS curves as well as Ramachandran probability maps, the original finite mixture approach RamaMix being developed for this second task. The similarity between profiles of local gyration radii provides to a certain extent a converged view of the Sic1 and pSic1 conformational space. Profiles and populations are thus proposed for describing IDP conformations. Different variations of the resulting gyration radius between phosphorylated and unphosphorylated states are observed, depending on the set of enumerated conformations as well as on the methods used for obtaining the populations.

Identifiants

pubmed: 36352011
doi: 10.1038/s41598-022-21648-9
pii: 10.1038/s41598-022-21648-9
pmc: PMC9646904
doi:

Substances chimiques

Intrinsically Disordered Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

19057

Subventions

Organisme : Agence Nationale de la Recherche
ID : ANR-19-CE45-0019

Informations de copyright

© 2022. The Author(s).

Références

Phys Rev E Stat Nonlin Soft Matter Phys. 2015 Mar;91(3):032712
pubmed: 25871149
J Bioinform Comput Biol. 2012 Jun;10(3):1242009
pubmed: 22809385
J Am Chem Soc. 2020 Sep 16;142(37):15697-15710
pubmed: 32840111
Nat Methods. 2020 Mar;17(3):261-272
pubmed: 32015543
Structure. 2010 Mar 14;18(4):494-506
pubmed: 20399186
Bioinformatics. 2013 Feb 1;29(3):398-9
pubmed: 23233655
Proc Natl Acad Sci U S A. 2007 Jun 5;104(23):9650-5
pubmed: 17522259
Nat Commun. 2022 Feb 10;13(1):793
pubmed: 35145092
Chem Rev. 2016 Jun 8;116(11):6424-62
pubmed: 26922996
J Appl Crystallogr. 2021 Feb 01;54(Pt 1):343-355
pubmed: 33833657
Nucleic Acids Res. 2021 Jan 8;49(D1):D404-D411
pubmed: 33305318
Sci Rep. 2021 Aug 19;11(1):16925
pubmed: 34413388
J Chem Theory Comput. 2019 May 14;15(5):3390-3401
pubmed: 30939006
J Chem Inf Model. 2014 Jan 27;54(1):289-301
pubmed: 24397493
J Phys Chem B. 2021 Jun 24;125(24):6451-6478
pubmed: 34115515
J Am Chem Soc. 2009 Dec 30;131(51):18314-26
pubmed: 20028147
Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17772-7
pubmed: 19008353
PLoS One. 2011;6(8):e23294
pubmed: 21887241
J Comput Chem. 2011 Jul 30;32(10):2319-27
pubmed: 21500218
Proc Natl Acad Sci U S A. 2008 Jul 1;105(26):8932-7
pubmed: 18579771
J Chem Inf Model. 2019 Oct 28;59(10):4486-4503
pubmed: 31442036
Nucleic Acids Res. 2008 Jan;36(Database issue):D402-8
pubmed: 17984079
Comput Biol Chem. 2013 Jun;44:22-30
pubmed: 23537565
Annu Rev Biochem. 2014;83:553-84
pubmed: 24606139
Bioinformatics. 2012 Jun 1;28(11):1463-70
pubmed: 22613562
Protein Sci. 2014 Sep;23(9):1275-90
pubmed: 24976112
Proteins. 2014 Sep;82(9):2157-68
pubmed: 24692201
Nature. 2020 Sep;585(7825):357-362
pubmed: 32939066
Structure. 2011 Jan 12;19(1):109-16
pubmed: 21220121
Structure. 2017 Nov 7;25(11):1645-1656.e5
pubmed: 28966015
Biochem J. 2021 Jun 11;478(11):2035-2050
pubmed: 34101805
Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):17002-7
pubmed: 16284250
J Am Chem Soc. 2010 Oct 27;132(42):14919-27
pubmed: 20925316
Methods Mol Biol. 2015;1260:17-32
pubmed: 25502373
Proteins. 2014 Mar;82(3):466-78
pubmed: 24038133
Arch Biochem Biophys. 2020 May 15;684:108342
pubmed: 32184088
Bioinformatics. 2011 Oct 15;27(20):2843-50
pubmed: 21873636

Auteurs

Daniel Förster (D)

UMR7374 Interfaces, Confinement, Matériaux et Nanostructures, Université d'Orléans, Orléans, France.

Jérôme Idier (J)

UMR6004 Laboratoire des Sciences du Numérique de Nantes, Nantes, France. jerome.idier@ls2n.fr.

Leo Liberti (L)

LIX UMR 7161 CNRS École Polytechnique, Institut Polytechnique de Paris, 91128, Palaiseau, France.

Antonio Mucherino (A)

IRISA, University of Rennes 1, Rennes, France.

Jung-Hsin Lin (JH)

Biomedical Translation Research Center, Academia Sinica, Taipei, Taiwan.

Thérèse E Malliavin (TE)

Institut Pasteur, Université Paris Cité, CNRS UMR3528, Unité de Bioinformatique Structurale, F-75015, Paris, France.
Université de Lorraine, CNRS UMR7019, LPCT, F-54000, Nancy, France.

Articles similaires

Silicon Dioxide Water Hot Temperature Compressive Strength X-Ray Diffraction
Cobalt Azo Compounds Ferric Compounds Polyesters Photolysis
1.00
Saccharomyces cerevisiae Lysine Cell Nucleolus RNA, Ribosomal Saccharomyces cerevisiae Proteins

Structural basis for molecular assembly of fucoxanthin chlorophyll

Koji Kato, Yoshiki Nakajima, Jian Xing et al.
1.00
Diatoms Photosystem I Protein Complex Chlorophyll Binding Proteins Cryoelectron Microscopy Light-Harvesting Protein Complexes

Classifications MeSH