Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Zanotti, Giuseppe | - |
| dc.creator | Vallese, Francesca | - |
| dc.creator | Ferrari, Alberto José | - |
| dc.creator | Menozzi, Ilaria | - |
| dc.creator | Saldaño, Tadeo Enrique | - |
| dc.creator | Berto, Paola | - |
| dc.creator | Fernández Alberti, Sebastián | - |
| dc.creator | Berni, Rodolfo | - |
| dc.date | 2018-04-10T13:36:07Z | - |
| dc.date | 2018-04-10T13:36:07Z | - |
| dc.date | 2017-12 | - |
| dc.date | 2018-04-09T15:19:38Z | - |
| dc.date.accessioned | 2019-04-29T15:42:04Z | - |
| dc.date.available | 2019-04-29T15:42:04Z | - |
| dc.date.issued | 2017-12 | - |
| dc.identifier | Zanotti, Giuseppe; Vallese, Francesca; Ferrari, Alberto José; Menozzi, Ilaria; Saldaño, Tadeo Enrique; et al.; Structural and dynamics evidence for scaffold asymmetric flexibility of the human transthyretin tetramer; Public Library of Science; Plos One; 12; 12; 12-2017 | - |
| dc.identifier | 1932-6203 | - |
| dc.identifier | http://hdl.handle.net/11336/41474 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/299890 | - |
| dc.description | The molecular symmetry of multimeric proteins is generally determined by using X-ray diffraction techniques, so that the basic question as to whether this symmetry is perfectly preserved for the same protein in solution remains open. In this work, human transthyretin (TTR), a homotetrameric plasma transport protein with two binding sites for the thyroid hormone thyroxine (T4), is considered as a case study. Based on the crystal structure of the TTR tetramer, a hypothetical D2 symmetry is inferred for the protein in solution, whose functional behavior reveals the presence of two markedly different Kd values for the two T4 binding sites. The latter property has been ascribed to an as yet uncharacterized negative binding cooperativity. A triple mutant form of human TTR (F87M/L110M/S117E TTR), which is monomeric in solution, crystallizes as a tetrameric protein and its structure has been determined. The exam of this and several other crystal forms of human TTR suggests that the TTR scaffold possesses a significant structural flexibility. In addition, TTR tetramer dynamics simulated using normal modes analysis exposes asymmetric vibrational patterns on both dimers and thermal fluctuations reveal small differences in size and flexibility for ligand cavities at each dimer-dimer interface. Such small structural differences between monomers can lead to significant functional differences on the TTR tetramer dynamics, a feature that may explain the functional heterogeneity of the T4 binding sites, which is partially overshadowed by the crystal state. | - |
| dc.description | Fil: Zanotti, Giuseppe. Università di Padova; Italia | - |
| dc.description | Fil: Vallese, Francesca. Università di Padova; Italia | - |
| dc.description | Fil: Ferrari, Alberto José. Università di Parma; Italia | - |
| dc.description | Fil: Menozzi, Ilaria. Università di Parma; Italia | - |
| dc.description | Fil: Saldaño, Tadeo Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina | - |
| dc.description | Fil: Berto, Paola. Università di Padova; Italia | - |
| dc.description | Fil: Fernández Alberti, Sebastián. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina | - |
| dc.description | Fil: Berni, Rodolfo. Università di Parma; Italia | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Public Library of Science | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1371/journal.pone.0187716 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0187716 | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.source.uri | http://hdl.handle.net/11336/34549 | - |
| dc.subject | TRANSTHYRETIN | - |
| dc.subject | X-RAY | - |
| dc.subject | NORMAL MODES | - |
| dc.subject | STRUCTURAL FLEXIBILITY | - |
| dc.subject | Otras Ciencias Biológicas | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Structural and dynamics evidence for scaffold asymmetric flexibility of the human transthyretin tetramer | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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