http://www.cnr.it/ontology/cnr/individuo/prodotto/ID9883
Two latent and two hyperstable polymeric forms of human neuroserpin (Articolo in rivista)
- Type
- Label
- Two latent and two hyperstable polymeric forms of human neuroserpin (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bpj.2010.09.021 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ricagno S.; Pezzullo M.; Barbiroli A.; Manno M.; Levantino M.; Santangelo M.G.; Bonomi F.; Bolognesi M. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- +Dipartimento di Scienze Biomolecolari e Biotecnologie, Centro Interdisciplinare Materiali e Interfacce Nanostrutturati, and
?Sezione di Biochimica, Dipartimento di Scienze Molecolari Agroalimentari, Universita` di Milano, Milan, Italy; §Dipartimento di Biochimica,
Universita` di Pavia, Pavia, Italy;
{
Laboratori di Biotecnologie, Istituto Di Ricovero e Cura a Carattere Scientifico Fondazione Policlinico
San Matteo, Pavia, Italy;
k
Istituto di Biofisica, Consiglio Nazionale delle Ricerche, CNR, Palermo, Italy; and **Dipartimento di Scienze Fisiche
ed Astronomiche, Universita` of Palermo, Palermo, Italy (literal)
- Titolo
- Two latent and two hyperstable polymeric forms of human neuroserpin (literal)
- Abstract
- Human neuroserpin (hNS) is a serine protease inhibitor that belongs to the serpin superfamily and is expressed in nervous tissues. The serpin fold is generally characterized by a long exposed loop, termed the reactive center loop, that acts as bait for the target protease. Intramolecular insertion of the reactive center loop into the main serpin ²-sheet leads to the serpin latent form. As with other known serpins, hNS pathological mutants have been shown to accumulate as polymers composed of quasi-native protein molecules. Although hNS polymerization has been intensely studied, a general agreement about serpin polymer organization is still lacking. Here we report a biophysical characterization of native hNS that is shown to undergo two distinct conformational transitions, at 55°C and 85°C, both leading to distinct latent and polymeric species. The latent and polymer hNS forms obtained at 45°C and 85°C differ in their chemical and thermal stabilities; furthermore, the hNS polymers also differ in size and morphology. Finally, the 85°C polymer shows a higher content of intermolecular ²-sheet interactions than the 45°C polymer. Together, these results suggest a more complex conformational scenario than was previously envisioned, and, in a general context, may help reconcile the current contrasting views on serpin polymerization. (literal)
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- Autore CNR
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