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- W2916403927 abstract "Abstract Neurotrypsin (NT) is a multi‐domain serine protease of the nervous system with only one known substrate: the large proteoglycan Agrin. NT has seen to be involved in the maintenance/turnover of neuromuscular junctions and in processes of synaptic plasticity in the central nervous system. Roles which have been tied to its enzymatic activity, localized in the C‐terminal serine‐protease (SP) domain. However the purpose of NT's remaining 3–4 scavenger receptor cysteine‐rich (SRCR) domains is still unclear. We have determined the crystal structure of the third SRCR domain of murine NT (mmNT‐SRCR3), immediately preceding the SP domain and performed a comparative structural analysis using homologous SRCR structures. Our data and the elevated degree of structural conservation with homologous domains highlight possible functional roles for NT SRCRs. Computational and experimental analyses suggest the identification of a putative binding region for Ca 2+ ions, known to regulate NT enzymatic activity. Furthermore, sequence and structure comparisons allow to single out regions of interest that, in future studies, might be implicated in Agrin recognition/binding or in interactions with as of yet undiscovered NT partners." @default.
- W2916403927 created "2019-03-02" @default.
- W2916403927 creator A5021215050 @default.
- W2916403927 creator A5066791837 @default.
- W2916403927 creator A5085654231 @default.
- W2916403927 date "2019-03-06" @default.
- W2916403927 modified "2023-10-16" @default.
- W2916403927 title "Structural characterization of the third scavenger receptor cysteine‐rich domain of murine neurotrypsin" @default.
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- W2916403927 doi "https://doi.org/10.1002/pro.3587" @default.
- W2916403927 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6423723" @default.
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- W2916403927 hasPublicationYear "2019" @default.
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