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PDBsum entry 1ntv
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Signaling protein
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PDB id
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1ntv
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 ptb domain complexes.
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Authors
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P.C.Stolt,
H.Jeon,
H.K.Song,
J.Herz,
M.J.Eck,
S.C.Blacklow.
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Ref.
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Structure, 2003,
11,
569-579.
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PubMed id
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Abstract
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Formation of the mammalian six-layered neocortex depends on a signaling pathway
that involves Reelin, the very low-density lipoprotein receptor, the
apolipoprotein E receptor-2 (ApoER2), and the adaptor protein Disabled-1 (Dab1).
The 1.5 A crystal structure of a complex between the Dab1 phosphotyrosine
binding (PTB) domain and a 14-residue peptide from the ApoER2 tail explains the
unusual preference of Dab1 for unphosphorylated tyrosine within the NPxY motif
of the peptide. Crystals of the complex soaked with the phosphoinositide
PI-4,5P(2) (PI) show that PI binds to conserved basic residues on the PTB domain
opposite the peptide binding groove. This finding explains how the Dab1 PTB
domain can simultaneously bind PI and the ApoER2 tail. Recruitment of the Dab1
PTB domain to PI-rich regions of the plasma membrane may facilitate association
with the Reelin receptor cytoplasmic tails to transduce a critical positional
cue to migrating neurons.
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