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PDBsum entry 4g2v
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Protein binding
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PDB id
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4g2v
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References listed in PDB file
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Key reference
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Title
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Structural and biochemical characterization of the interaction between lgn and frmpd1.
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Authors
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Z.Pan,
Y.Shang,
M.Jia,
L.Zhang,
C.Xia,
M.Zhang,
W.Wang,
W.Wen.
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Ref.
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J Mol Biol, 2013,
425,
1039-1049.
[DOI no: ]
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PubMed id
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Abstract
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The tetratricopeptide repeat (TPR) motif-containing protein LGN binds multiple
targets and regulates their subcellular localizations and functions during both
asymmetric and symmetric cell divisions. Here, we characterized the interaction
between LGN-TPR motifs and FERM and PDZ domain containing 1 (Frmpd1) and
reported the crystal structure of the complex at 2.4Å resolution. A highly
conserved fragment at the center of Frmpd1 of ~20 residues was found to be
necessary and sufficient to bind to LGN-TPR. This Frmpd1 fragment forms an
extended structure and runs along the concave channel of the TPR superhelix in
an antiparallel manner in the complex. Structural comparisons and biochemical
studies of LGN/Frmpd1 and other known LGN/target interactions demonstrate that
the LGN-TPR motifs are versatile and capable of recognizing multiple targets via
diverse binding modes. Nevertheless, a conserved
"E/QxEx4-5E/D/Qx1-2K/R" motif in LGN/Pins (partner of inscuteable) TPR
binding proteins has been identified.
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