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PDBsum entry 1kyu
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Endocytosis/exocytosis
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PDB id
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1kyu
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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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Accessory protein recruitment motifs in clathrin-Mediated endocytosis.
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Authors
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T.J.Brett,
L.M.Traub,
D.H.Fremont.
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Ref.
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Structure, 2002,
10,
797-809.
[DOI no: ]
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PubMed id
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Abstract
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Clathrin-mediated endocytosis depends upon the interaction of accessory proteins
with the alpha-ear of the AP-2 adaptor. We present structural characterization
of these regulatory interactions. DPF and DPW motif peptides derived from eps15
and epsin bind in type I beta turn conformations to a conserved pocket on the
alpha-ear platform. We show evidence for a second binding site that is DPW motif
specific. The structure of a complex with an AP-2 binding segment from
amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged
in an extended conformation by a unique surface of the platform domain. The
FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and
can be found in several potential endocytic proteins, including HIP1, CD2AP, and
PLAP. A mechanism of clathrin assembly regulation is suggested by three
different AP-2 engagement modes.
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Figure 1.
Figure 1. Experimental Evidence for DPF, DPW, and FxDxF
Motif Peptides Binding to the a-Ear(A) Ribbon representation of
the a-ear showing the binding sites of the FxDxF (extended
platform site) and DPW2 (distal site) peptides, with the
peptides shown as CPK models.(B-E) The fit of each peptide to
its corresponding simulated annealing omit electron density
contoured at 2.5 s.(B) The FxDxF peptide at 2.15 Å
resolution.(C) The DPF peptide (in P2[1]) at 1.22 Å
resolution.(D) The DPW1 peptide at 2.0 Å resolution.(E) The DPW2
peptide at 2.0 Å resolution. The orientation of the peptides
depicted in B, C, and D were achieved by superposition of the
a-ear platform domain. For the DPW2 peptide in (E), the Ca
coordinates were aligned with those of the DPF peptide. DPF,
cyan; DPW1, steel blue; DPW2, blue-green; FxDxF, magenta.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
797-809)
copyright 2002.
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