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PDBsum entry 2dc2
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Structural protein
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PDB id
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2dc2
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References listed in PDB file
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Key reference
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Title
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Solution structure of gopc pdz domain and its interaction with the c-Terminal motif of neuroligin.
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Authors
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X.Li,
J.Zhang,
Z.Cao,
J.Wu,
Y.Shi.
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Ref.
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Protein Sci, 2006,
15,
2149-2158.
[DOI no: ]
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PubMed id
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Abstract
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GOPC (Golgi-associated PDZ and coiled-coil motif-containing protein) represents
a PDZ domain-containing protein associated with the Golgi apparatus, which plays
important roles in vesicular trafficking in secretory and endocytic pathways.
GOPC interacts with many other proteins, such as the Wnt receptors Frizzled 8
and neuroligin via its PDZ domain. Neuroligin is a neural cell-adhesion molecule
of the post-synapse, which binds to the presynapse molecule neurexin to form a
heterotypic intercellular junction. Here we report the solution structure of the
GOPC PDZ domain by NMR. Our results show that it is a canonical class I PDZ
domain, which contains two alpha-helices and six beta-strands. Using chemical
shift perturbation experiments, we further studied the binding properties of the
GOPC PDZ domain with the C-terminal motif of neuroligin. The observations showed
that the ensemble of the interaction belongs to fast exchange with low affinity.
The 3D model of the GOPC PDZ domain/neuroligin C-terminal peptide complex was
constructed with the aid of the molecular dynamics simulation method. Our
discoveries provide insight into the specific interaction of the GOPC PDZ domain
with the C-terminal peptide of Nlg and also provide a general insight about the
possible binding mode of the interaction of Nlg with other PDZ domain-containing
proteins.
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Figure 4.
Figure 4. Histogram showing differences in chemical shifts in the free
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Figure 6.
Figure 6. Nlg-binding site on the surface of the GOPC PDZ domain. (A) Surface conformation of the GOPC PDZ domain
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2006,
15,
2149-2158)
copyright 2006.
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