ArticleBiochimica et biophysica acta2015
Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics.
Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Neuroserpin: structure, function, physiology and pathology.Cellular and molecular life sciences : CMLS · 2021Review
- Scaling Concepts in Serpin Polymer Physics.Materials (Basel, Switzerland) · 2021Article
- N-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function.International journal of molecular sciences · 2021Article
- Embelin as Lead Compound for New Neuroserpin Polymerization Inhibitors.Life (Basel, Switzerland) · 2020Article
- Glycosylation Tunes Neuroserpin Physiological and Pathological Properties.International journal of molecular sciences · 2020Article
- Conformational preludes to the latency transition in PAI-1 as determined by atomistic computer simulations and hydrogen/deuterium-exchange mass spectrometry.Scientific reports · 2017Article
- A hydrophobic patch surrounding Trp154 in human neuroserpin controls the helix F dynamics with implications in inhibition and aggregation.Scientific reports · 2017Article
- Embelin binds to human neuroserpin and impairs its polymerisation.Scientific reports · 2016Article
- Interactions between N-linked glycosylation and polymerisation of neuroserpin within the endoplasmic reticulum.The FEBS journal · 2015Article
- The stability and activity of human neuroserpin are modulated by a salt bridge that stabilises the reactive centre loop.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
Neuroserpin (NS) is a serine protease inhibitor (SERPIN) involved in different neurological pathologies, including the Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB), related to the aberrant polymerization of NS mutants. Here we present an in vitro and in silico characterization of native neuroserpin and its dysfunctional conformation isoforms: the proteolytically cleaved conformer, the inactive latent conformer, and the polymeric species. Based on circular dichroism and fluorescence spectroscopy, we present an experimental validation of the latent model and highlight the main structural features of the different conformers. In particular, emission spectra of aromatic residues yield distinct conformational fingerprints, that provide a novel and simple spectroscopic tool for selecting serpin conformers in vitro. Based on the structural relationship between cleaved and latent serpins, we propose a structural model for latent NS, for which an experimental crystallographic structure is lacking. Molecular Dynamics simulations suggest that NS conformational stability and flexibility arise from a spatial distribution of intramolecular salt-bridges and hydrogen bonds.
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