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For the record: A logical sequence search for S100B target proteins
Author(s) -
Mcclintock Kimberly A.,
Shaw Gary S.
Publication year - 2000
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.9.10.2043
Subject(s) - desmin , intermediate filament , tubulin , vimentin , biology , glial fibrillary acidic protein , consensus sequence , conserved sequence , sequence (biology) , peptide sequence , neurofilament , calcium binding protein , cytoskeleton , microbiology and biotechnology , biochemistry , chemistry , microtubule , calcium , gene , immunohistochemistry , organic chemistry , cell , immunology
The EF‐hand calcium‐binding protein S100B has been shown to interact in vitro in a calcium‐sensitive manner with many substrates. These potential S100B target proteins have been screened for the preservation of a previously identified consensus sequence across species. The results were compared to known structural and in vitro properties of the proteins to rationalize choices for potential binding partners. Our approach uncovered four oligomeric proteins tubulin (α and β), glial fibrillary acidic protein (GFAP), desmin, and vimentin that have conserved regions matching the consensus sequence. In the type III intermediate filament proteins (GFAP, vimentin, and desmin), this region corresponds to a portion of a coiled‐coil (helix 2A), the structural element responsible for their assembly. In tubulin, the sequence matches correspond to regions of α and β tubulin found at the αβ tubulin interface. In both cases, these consensus sequence matches provide a logical explanation for in vitro observations that S100B is able to inhibit oligomerization of these proteins.