PDBsum entry 1g3j

Transcription

PDB id: 1g3j

Contents

Protein chains

522 a.a. *

41 a.a. *

439 a.a. *

34 a.a. *

Waters ×263

* Residue conservation analysis

References listed in PDB file

Key reference

Title

Crystal structure of a beta-Catenin/tcf complex.

Authors

T.A.Graham, C.Weaver, F.Mao, D.Kimelman, W.Xu.

Ref.

Cell, 2000, 103, 885-896. [DOI no: 10.1016/S0092-8674(00)00192-6]

PubMed id

11136974

Abstract

The Wnt signaling pathway plays critical roles in embryonic development and tumorigenesis. Stimulation of the Wnt pathway results in the accumulation of a nuclear beta-catenin/Tcf complex, activating Wnt target genes. A crystal structure of beta-catenin bound to the beta-catenin binding domain of Tcf3 (Tcf3-CBD) has been determined. The Tcf3-CBD forms an elongated structure with three binding modules that runs antiparallel to beta-catenin along the positively charged groove formed by the armadillo repeats. Structure-based mutagenesis defines three sites in beta-catenin that are critical for binding the Tcf3-CBD and are differentially involved in binding APC, cadherin, and Axin. The structural and mutagenesis data reveal a potential target for molecular drug design studies.

Figure 3.
Figure 3. The Interactions between β-Catenin and the β Strand in the Extended Region of XTcf3-CBD(A) Stereo 2F[o]−F[c] simulated annealed omit map of XTcf3-CBD. XTcf3 residues are denoted in yellow and β-catenin residues are denoted in red. Solvent molecules are shown in turquoise. The map is shown at a level of 1σ.(B) Structure of the XTcf3 extended region on the top of the β-catenin molecular surface. Two semi-buried charged buttons, Lys-435 and Lys-312, are critical for the β-catenin/Tcf interactions. The β-catenin surface was cut off in the upper part of the figure to be able to view the extended region of XTcf3-CBD. XTcf3 residues are shown in white and exposed β-catenin residues due to the cut surface are shown in green. XTcf3 residues are labeled in yellow and β-catenin residues are labeled in white. The equipotential contours at the relative levels of 10, 20, 30, 40, and 50 were calculated with GRASP and are shown in white.(C) XTcf3 extended region bonding diagram. The same conventions are used as in Figure 2B.

Figure 4.
Figure 4. The Interactions between β-Catenin and the XTcf3-CBD Helix(A) Molecular model of the XTcf3 helical region. XTcf3 residues are labeled in yellow and β-catenin residues are labeled in white.(B) XTcf3 helix module bonding diagram. The same conventions are used as in Figure 2B.

The above figures are reprinted by permission from Cell Press: Cell (2000, 103, 885-896) copyright 2000.