Campus Event Calendar
Event Entry
What and Who
Predicting molecular details for protein interaction networks
Victor Neduva
EMBL Heidelberg
Talk
AG 1, AG 2, AG 3, AG 4, AG 5, SWS
AG Audience
English
Note: We use this to send email in the morning.
Date, Time and Location
Wednesday, 25 October 2006
15:00
-- Not specified --
E1 4
021
Saarbrücken
Abstract
The abstract: "Many aspects of cell signaling, trafficking and targeting
are governed by interactions between globular protein domains and short
peptide segments. These domains often bind multiple peptides with a
common sequence pattern, or linear motif (e.g. SH3 binding to PxxP).
Many domains are known, though comparatively few linear motifs have been
discovered. Their short length (3-8 residues), and the fact that they
often reside in disordered regions in proteins makes them difficult to
detect by sequence comparison, or to study experimentally. Nevertheless,
each new motif provides critical molecular details of how interaction
networks are constructed, and can explain how one protein is able bind
to very different partners. We show that output from genome-scale
interaction studies can be used to detect linear motifs, and thus avoid
the normally slow discovery process. Our approach re-discovers known
motifs and predicts dozens of others. Direct binding experiments reveal
that two predicted motifs are indeed protein-binding modules. More
extensive studies to verify human linear motifs are underway in our lab.
Our results suggest that there are likely hundreds of linear-motifs yet
to be discovered that could greatly illuminate cellular processes."
are governed by interactions between globular protein domains and short
peptide segments. These domains often bind multiple peptides with a
common sequence pattern, or linear motif (e.g. SH3 binding to PxxP).
Many domains are known, though comparatively few linear motifs have been
discovered. Their short length (3-8 residues), and the fact that they
often reside in disordered regions in proteins makes them difficult to
detect by sequence comparison, or to study experimentally. Nevertheless,
each new motif provides critical molecular details of how interaction
networks are constructed, and can explain how one protein is able bind
to very different partners. We show that output from genome-scale
interaction studies can be used to detect linear motifs, and thus avoid
the normally slow discovery process. Our approach re-discovers known
motifs and predicts dozens of others. Direct binding experiments reveal
that two predicted motifs are indeed protein-binding modules. More
extensive studies to verify human linear motifs are underway in our lab.
Our results suggest that there are likely hundreds of linear-motifs yet
to be discovered that could greatly illuminate cellular processes."
Contact
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Ruth Schneppen-Christmann, 10/19/2006 11:09 -- Created document.