Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease
Open Access
- 20 August 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 505 (1) , 18-22
- https://doi.org/10.1016/s0014-5793(01)02764-8
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 β‐sheet A, an essential step in the inhibition and possibly in the polymerization of neuroserpin.Keywords
This publication has 32 references indexed in Scilit:
- Solvent content of protein crystalsPublished by Elsevier ,2006
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Human Neuroserpin (PI12): cDNA Cloning and Chromosomal Localization to 3q26Genomics, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Crystal Structure of Cleaved Bovine Antithrombin III at 3·2 Å ResolutionJournal of Molecular Biology, 1993
- SETOR: Hardware-lighted three-dimensional solid model representations of macromoleculesJournal of Molecular Graphics, 1993
- Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1·95Å resolutionJournal of Molecular Biology, 1992
- Crystal structure of uncleaved ovalbumin at 1·95 Å resolutionJournal of Molecular Biology, 1991
- Crystal structure of cleaved human α1-antichymotrypsin at 2.7 å resolution and its comparison with other serpinsJournal of Molecular Biology, 1991