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Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease.


Briand, C; Kozlov, S V; Sonderegger, P; Grütter, M G (2001). Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease. FEBS Letters, 505(1):18-22.

Abstract

The protease inhibitor neuroserpin regulates the development of the nervous system and its plasticity in the adult. Neuroserpins carrying the Ser53Pro or Ser56Arg mutation form polymers in neuronal cells. We describe here the structure of wild-type neuroserpin in a cleaved form. The structure provides a basis to understand the role of the mutations in the polymerization process. We propose that these mutations could delay the insertion of the reactive center loop into the central beta-sheet A, an essential step in the inhibition and possibly in the polymerization of neuroserpin.

Abstract

The protease inhibitor neuroserpin regulates the development of the nervous system and its plasticity in the adult. Neuroserpins carrying the Ser53Pro or Ser56Arg mutation form polymers in neuronal cells. We describe here the structure of wild-type neuroserpin in a cleaved form. The structure provides a basis to understand the role of the mutations in the polymerization process. We propose that these mutations could delay the insertion of the reactive center loop into the central beta-sheet A, an essential step in the inhibition and possibly in the polymerization of neuroserpin.

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Additional indexing

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Uncontrolled Keywords:Serpin, Protease inhibitor, Crystal structure, Polymerization
Language:English
Date:7 September 2001
Deposited On:11 Feb 2008 12:20
Last Modified:18 Apr 2018 11:38
Publisher:Elsevier
ISSN:0014-5793
Funders:Baugartenstiftung, Association pour la Recherche contre le Cancer.
OA Status:Closed
Publisher DOI:https://doi.org/10.1016/S0014-5793(01)02764-8
PubMed ID:11557034

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