Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein
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...
Guardado en:
| Autores principales: | , , , , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00426822_v525_n_p117_Glavina |
| Aporte de: |
| id |
todo:paper_00426822_v525_n_p117_Glavina |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_00426822_v525_n_p117_Glavina2023-10-03T14:51:27Z Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein Glavina, J. Román, E.A. Espada, R. de Prat-Gay, G. Chemes, L.B. Sánchez, I.E. Adenovirus Co-evolution E1A Intrinsic disorder Linear motifs Motif repertoire Random polymer Sequence conservation E1A protein intrinsically disordered protein E1A protein amino acid sequence Article coevolution conserved sequence controlled study Human adenovirus 12 Human adenovirus 5 nonhuman priority journal protein binding protein conformation protein domain protein motif protein protein interaction protein structure amino acid sequence chemistry genetics human Human adenovirus C metabolism protein motif translational protein modification Adenovirus E1A Proteins Adenoviruses, Human Amino Acid Motifs Amino Acid Sequence Humans Protein Conformation Protein Domains Protein Modification, Translational 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00426822_v525_n_p117_Glavina |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Adenovirus Co-evolution E1A Intrinsic disorder Linear motifs Motif repertoire Random polymer Sequence conservation E1A protein intrinsically disordered protein E1A protein amino acid sequence Article coevolution conserved sequence controlled study Human adenovirus 12 Human adenovirus 5 nonhuman priority journal protein binding protein conformation protein domain protein motif protein protein interaction protein structure amino acid sequence chemistry genetics human Human adenovirus C metabolism protein motif translational protein modification Adenovirus E1A Proteins Adenoviruses, Human Amino Acid Motifs Amino Acid Sequence Humans Protein Conformation Protein Domains Protein Modification, Translational |
| spellingShingle |
Adenovirus Co-evolution E1A Intrinsic disorder Linear motifs Motif repertoire Random polymer Sequence conservation E1A protein intrinsically disordered protein E1A protein amino acid sequence Article coevolution conserved sequence controlled study Human adenovirus 12 Human adenovirus 5 nonhuman priority journal protein binding protein conformation protein domain protein motif protein protein interaction protein structure amino acid sequence chemistry genetics human Human adenovirus C metabolism protein motif translational protein modification Adenovirus E1A Proteins Adenoviruses, Human Amino Acid Motifs Amino Acid Sequence Humans Protein Conformation Protein Domains Protein Modification, Translational Glavina, J. Román, E.A. Espada, R. de Prat-Gay, G. Chemes, L.B. Sánchez, I.E. Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein |
| topic_facet |
Adenovirus Co-evolution E1A Intrinsic disorder Linear motifs Motif repertoire Random polymer Sequence conservation E1A protein intrinsically disordered protein E1A protein amino acid sequence Article coevolution conserved sequence controlled study Human adenovirus 12 Human adenovirus 5 nonhuman priority journal protein binding protein conformation protein domain protein motif protein protein interaction protein structure amino acid sequence chemistry genetics human Human adenovirus C metabolism protein motif translational protein modification Adenovirus E1A Proteins Adenoviruses, Human Amino Acid Motifs Amino Acid Sequence Humans Protein Conformation Protein Domains Protein Modification, Translational |
| description |
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. |
| format |
JOUR |
| author |
Glavina, J. Román, E.A. Espada, R. de Prat-Gay, G. Chemes, L.B. Sánchez, I.E. |
| author_facet |
Glavina, J. Román, E.A. Espada, R. de Prat-Gay, G. Chemes, L.B. Sánchez, I.E. |
| author_sort |
Glavina, J. |
| title |
Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein |
| title_short |
Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein |
| title_full |
Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein |
| title_fullStr |
Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein |
| title_full_unstemmed |
Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein |
| title_sort |
interplay between sequence, structure and linear motifs in the adenovirus e1a hub protein |
| url |
http://hdl.handle.net/20.500.12110/paper_00426822_v525_n_p117_Glavina |
| work_keys_str_mv |
AT glavinaj interplaybetweensequencestructureandlinearmotifsintheadenoviruse1ahubprotein AT romanea interplaybetweensequencestructureandlinearmotifsintheadenoviruse1ahubprotein AT espadar interplaybetweensequencestructureandlinearmotifsintheadenoviruse1ahubprotein AT depratgayg interplaybetweensequencestructureandlinearmotifsintheadenoviruse1ahubprotein AT chemeslb interplaybetweensequencestructureandlinearmotifsintheadenoviruse1ahubprotein AT sanchezie interplaybetweensequencestructureandlinearmotifsintheadenoviruse1ahubprotein |
| _version_ |
1807323167323062272 |