Structural highlights
Function
[NEUS_MOUSE] Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease.,Briand C, Kozlov SV, Sonderegger P, Grutter MG FEBS Lett. 2001 Sep 7;505(1):18-22. PMID:11557034[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Briand C, Kozlov SV, Sonderegger P, Grutter MG. Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease. FEBS Lett. 2001 Sep 7;505(1):18-22. PMID:11557034
