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The NTR module: Domains of netrins, secreted frizzled related proteins, and type I procollagen C‐proteinase enhancer protein are homologous with tissue inhibitors of metalloproteases
Author(s) -
Bányai László,
Patthy László
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.8.1636
Subject(s) - metalloproteinase , biology , microbiology and biotechnology , procollagen peptidase , enhancer , netrin , frizzled , matrix metalloproteinase , biochemistry , gene , wnt signaling pathway , signal transduction , axon guidance , gene expression , axon
Using homology search, structure prediction, and structural characterization methods we show that the C‐terminal domains of (1) netrins, (2) complement proteins C3, C4, C5, (3) secreted frizzled‐related proteins, and (4) type I procollagen C‐proteinase enhancer proteins (PCOLCEs) are homologous with the N‐terminal domains of (5) tissue inhibitors of metalloproteinases (TIMPs). The proteins harboring this netrin module (NTR module) fulfill diverse biological roles ranging from axon guidance, regulation of Wnt signaling, to the control of the activity of metalloproteases. With the exception of TIMPs, it is not known at present what role the NTR modules play in these processes. In view of the fact that the NTR modules of TIMPs are involved in the inhibition of matrixin‐type metalloproteases and that the NTR module of PCOLCEs is involved in the control of the activity of the astacin‐type metalloprotease BMP1, it seems possible that interaction with metzincins could be a shared property of NTR modules and could be critical for the biological roles of the host proteins.