Interaction between the internal motif KTXXXI of Idax and mDvl PDZ domain.

Abstract:

:Dishevelled (Dvl) is the essential signal transduction component of both canonical and non-canonical Wnt signaling pathways. The cysteine-rich protein Idax acts as a negative regulator of Wnt signaling in mammals by interaction with Dvl in the region of the PDZ domain. In an effort to clarify the structural basis of this interaction, we used nuclear magnetic resonance spectroscopy to study the interaction of the Dvl PDZ domain with Idax. We first confirmed that the C-terminal region of Idax consisting of residues 109-198 binds to the PDZ domain of mouse Dvl-1 at the conventional C-terminal peptide-binding groove. However, instead of the C-terminus of Idax, we showed that a peptide of an internal sequence of Idax containing a KTXXXI motif is important in the interaction with a binding affinity estimated at 56 microM. Such internal motif identified in this study suggests a new type of sequence motif recognition for Dvl PDZ domain.

authors

London TB,Lee HJ,Shao Y,Zheng J

doi

10.1016/j.bbrc.2004.07.113

subject

Has Abstract

pub_date

2004-09-10 00:00:00

pages

326-32

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)01582-7

journal_volume

322

pub_type

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