Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein

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E1A is the main transforming protein in mastadenoviruses. This work uses bioinformatics to extrapolate experimental knowledge from Human adenovirus serotype 5 and 12 E1A proteins to all known serotypes. A conserved domain architecture with a high degree of intrinsic disorder acts as a scaffold for m...

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Autor principal: Glavina, J.
Otros Autores: Román, E.A, Espada, R., de Prat-Gay, G., Chemes, L.B, Sánchez, I.E
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Academic Press Inc. 2018
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 cas  |a Adenovirus E1A Proteins 
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100 1 |a Glavina, J. 
245 1 0 |a Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein 
260 |b Academic Press Inc.  |c 2018 
270 1 0 |m Chemes, L.B.; Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas IIB-INTECH, Universidad Nacional de San Martín, San MartínArgentina; email: lchemes@iib.unsam.edu.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a E1A is the main transforming protein in mastadenoviruses. This work uses bioinformatics to extrapolate experimental knowledge from Human adenovirus serotype 5 and 12 E1A proteins to all known serotypes. A conserved domain architecture with a high degree of intrinsic disorder acts as a scaffold for multiple linear motifs with variable occurrence mediating the interaction with over fifty host proteins. While linear motifs contribute strongly to sequence conservation within intrinsically disordered E1A regions, motif repertoires can deviate significantly from those found in prototypical serotypes. Close to one hundred predicted residue-residue contacts suggest the presence of stable structure in the CR3 domain and of specific conformational ensembles involving both short- and long-range intramolecular interactions. Our computational results suggest that E1A sequence conservation and co-evolution reflect the evolutionary pressure to maintain a mainly disordered, yet non-random conformation harboring a high number of binding motifs that mediate viral hijacking of the cell machinery. © 2018 Elsevier Inc.  |l eng 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, PICT 2015-1213, PICT 2012-2550 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: PIP 2014-2016 11220130100558CO 
536 |a Detalles de la financiación: PICT 2013-1895 
536 |a Detalles de la financiación: We acknowledge funding from  Agencia Nacional de Promoción Científica y Tecnológica ( PICT 2012-2550 and PICT 2015-1213 to I.E.S. and PICT 2013-1895 to L.B.C.), Consejo Nacional de Investigaciones Científicas y Técnicas (Graduate fellowship to J.G. and R.E.; L.B.C., G.d.P.G., E.A.R. and I.E.S. are CONICET career investigators, L.B.C. is the recipient of PIP 2014-2016 11220130100558CO ). Help from Alan Bush with statistical analyses is gratefully acknowledged. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Appendix A 
593 |a Universidad de Buenos Aires. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales (IQUIBICEN). Facultad de Ciencias Exactas y Naturales. Laboratorio de Fisiología de Proteínas, Buenos Aires, Argentina 
593 |a Instituto de Química y Físico-Química Biológicas, Universidad de Buenos Aires, Junín 956, Buenos Aires, 1113AAD, Argentina 
593 |a Protein Structure-Function and Engineering Laboratory, Fundación Instituto Leloir and IIBBA-CONICET, Buenos Aires, Argentina 
593 |a Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Biotecnológicas IIB-INTECH, Universidad Nacional de San Martín, San Martín, Buenos Aires, Argentina 
593 |a Departamento de Fisiología y Biología Molecular y Celular (DFBMC), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina 
690 1 0 |a ADENOVIRUS 
690 1 0 |a CO-EVOLUTION 
690 1 0 |a E1A 
690 1 0 |a INTRINSIC DISORDER 
690 1 0 |a LINEAR MOTIFS 
690 1 0 |a MOTIF REPERTOIRE 
690 1 0 |a RANDOM POLYMER 
690 1 0 |a SEQUENCE CONSERVATION 
690 1 0 |a E1A PROTEIN 
690 1 0 |a INTRINSICALLY DISORDERED PROTEIN 
690 1 0 |a E1A PROTEIN 
690 1 0 |a AMINO ACID SEQUENCE 
690 1 0 |a ARTICLE 
690 1 0 |a COEVOLUTION 
690 1 0 |a CONSERVED SEQUENCE 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a HUMAN ADENOVIRUS 12 
690 1 0 |a HUMAN ADENOVIRUS 5 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN CONFORMATION 
690 1 0 |a PROTEIN DOMAIN 
690 1 0 |a PROTEIN MOTIF 
690 1 0 |a PROTEIN PROTEIN INTERACTION 
690 1 0 |a PROTEIN STRUCTURE 
690 1 0 |a AMINO ACID SEQUENCE 
690 1 0 |a CHEMISTRY 
690 1 0 |a GENETICS 
690 1 0 |a HUMAN 
690 1 0 |a HUMAN ADENOVIRUS C 
690 1 0 |a METABOLISM 
690 1 0 |a PROTEIN MOTIF 
690 1 0 |a TRANSLATIONAL PROTEIN MODIFICATION 
690 1 0 |a ADENOVIRUS E1A PROTEINS 
690 1 0 |a ADENOVIRUSES, HUMAN 
690 1 0 |a AMINO ACID MOTIFS 
690 1 0 |a AMINO ACID SEQUENCE 
690 1 0 |a HUMANS 
690 1 0 |a PROTEIN CONFORMATION 
690 1 0 |a PROTEIN DOMAINS 
690 1 0 |a PROTEIN MODIFICATION, TRANSLATIONAL 
700 1 |a Román, E.A. 
700 1 |a Espada, R. 
700 1 |a de Prat-Gay, G. 
700 1 |a Chemes, L.B. 
700 1 |a Sánchez, I.E. 
773 0 |d Academic Press Inc., 2018  |g v. 525  |h pp. 117-131  |p Virology  |x 00426822  |w (AR-BaUEN)CENRE-2  |t Virology 
856 4 1 |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-85053763490&doi=10.1016%2fj.virol.2018.08.012&partnerID=40&md5=c405a14d92a0aeed2b30acc3251fbcd2  |y Registro en Scopus 
856 4 0 |u https://doi.org/10.1016/j.virol.2018.08.012  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00426822_v525_n_p117_Glavina  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00426822_v525_n_p117_Glavina  |y Registro en la Biblioteca Digital 
961 |a paper_00426822_v525_n_p117_Glavina  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
999 |c 85892 

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