Hostname: page-component-586b7cd67f-2brh9 Total loading time: 0 Render date: 2024-12-01T01:52:29.002Z Has data issue: false hasContentIssue false
  • English
  • Français

A novel clan of zinc metallopeptidases with possible intramembrane cleavage properties

Published online by Cambridge University Press:  01 February 1999

ALAN P. LEWIS  and
PAM J. THOMAS
ALAN P. LEWIS
Affiliation:
Advanced Technology and Informatics Unit, GlaxoWellcome Medicines Research Centre, Stevenage SG1 2NY, United Kingdom
PAM J. THOMAS
Affiliation:
Biomolecular Structure Unit, GlaxoWellcome Medicines Research Centre, Stevenage SG1 2NY, United Kingdom
Get access

Abstract

Computer-based database searching and protein multiple sequence alignment has identified a novel clan of zinc metallopeptidases, which, by phylogenetic analysis, has been shown to contain six subfamilies. The family is characterized by four common transmembrane segments and three conserved sequence motifs. The combination of topology analysis and motif identification has detected three potential Zn2+ coordinating residues. Only two of the sequences of this novel zinc metallopeptidase clan possess any functional annotation, one of which is able to cleave its substrate within a cytosol/transmembrane segment junction. A number of observations suggest that the remaining members of this novel clan may also cleave their substrates within transmembrane segments.

Keywords

homology searchintramembrane cleavageprotein familytransmembrane proteinzinc metallopeptidase
Type
FOR THE RECORD
Information
Protein Science , Volume 8 , Issue 2 , February 1999 , pp. 439 - 442
Copyright
© 1999 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.)