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PDBsum entry 4wnd
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Signaling protein/protein binding
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PDB id
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4wnd
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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 basis for the recognition of the scaffold protein frmpd4/preso1 by the tpr domain of the adaptor protein lgn.
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Authors
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H.Takayanagi,
S.Yuzawa,
H.Sumimoto.
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Ref.
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Acta Crystallogr F Struct Biol Commun, 2015,
71,
175-183.
[DOI no: ]
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PubMed id
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Abstract
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The adaptor protein LGN interacts via the N-terminal domain comprising eight
tetratricopeptide-repeat (TPR) motifs with its partner proteins mInsc, NuMA,
Frmpd1 and Frmpd4 in a mutually exclusive manner. Here, the crystal structure of
the LGN TPR domain in complex with human Frmpd4 is described at 1.5 Å
resolution. In the complex, the LGN-binding region of Frmpd4 (amino-acid
residues 990-1011) adopts an extended structure that runs antiparallel to LGN
along the concave surface of the superhelix formed by the TPR motifs. Comparison
with the previously determined structures of the LGN-Frmpd1, LGN-mInsc and
LGN-NuMA complexes reveals that these partner proteins interact with LGN TPR1-6
via a common core binding region with consensus sequence
(E/Q)XEX4-5(E/D/Q)X1-2(K/R)X0-1(V/I). In contrast to Frmpd1, Frmpd4 makes
additional contacts with LGN via regions N- and C-terminal to the core sequence.
The N-terminal extension is replaced by a specific α-helix in mInsc, which
drastically increases the direct contacts with LGN TPR7/8, consistent with the
higher affinity of mInsc for LGN. A crystal structure of Frmpd4-bound LGN in an
oxidized form is also reported, although oxidation does not appear to strongly
affect the interaction with Frmpd4.
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