Hostname: page-component-586b7cd67f-rcrh6 Total loading time: 0 Render date: 2024-11-24T13:25:43.122Z Has data issue: false hasContentIssue false
  • English
  • Français

A logical sequence search for S100B target proteins

Published online by Cambridge University Press:  15 December 2000

KIMBERLY A. McCLINTOCK  and
GARY S. SHAW
KIMBERLY A. McCLINTOCK
Affiliation:
Department of Biochemistry and McLaughlin Macromolecular Structure Facility, The University of Western Ontario, London, Ontario N6A 5C1, Canada
GARY S. SHAW
Affiliation:
Department of Biochemistry and McLaughlin Macromolecular Structure Facility, The University of Western Ontario, London, Ontario N6A 5C1, Canada
Get access

Abstract

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.

Keywords

calcium-binding proteinEF-handprotein interactionsS100TRTK-12
Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 10 , October 2000 , pp. 2043 - 2046
Copyright
© 2000 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)