Protein Engineering, Vol 11, 1155-1161, Copyright © 1998 by Oxford University Press
B Eisenhaber, P Bork and F Eisenhaber
Glycosylphosphatidylinositol (GPI) anchoring is a common post-
translational modification of extracellular eukaryotic proteins. Attachment
of the GPI moiety to the carboxyl terminus (omega-site) of the polypeptide
occurs after proteolytic cleavage of a C-terminal propeptide. In this work,
the sequence pattern for GPI-modification was analyzed in terms of physical
amino acid properties based on a database analysis of annotated proprotein
sequences. In addition to a refinement of previously described sequence
signals, we report conserved sequence properties in the regions omega -
11...omega - 1 and omega + 4...omega + 5. We present statistical evidence
for volume-compensating residue exchanges with respect to the positions
omega - 1...omega + 2. Differences between protozoan and metazoan
GPI-modification motifs consist mainly in variations of preferences to
amino acid types at the positions near the omega-site and in the overall
motif length. The variations of polypeptide substrates are exploited to
suggest a model of the polypeptide binding site of the putative
transamidase, the enzyme catalyzing the GPI-modification. The volume of the
active site cleft accommodating the four residues omega - 1...omega + 2
appears to be approximately 540 A3.
ARTICLES
Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase
European Molecular Biology Laboratory, Heidelberg, Germany. birgit.eisenhaber@embl-heidelberg.de
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