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PDBsum entry 2he2
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Signaling protein
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PDB id
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2he2
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References listed in PDB file
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Key reference
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Title
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Structure of pick1 and other pdz domains obtained with the help of self-Binding c-Terminal extensions.
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Authors
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J.M.Elkins,
E.Papagrigoriou,
G.Berridge,
X.Yang,
C.Phillips,
C.Gileadi,
P.Savitsky,
D.A.Doyle.
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Ref.
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Protein Sci, 2007,
16,
683-694.
[DOI no: ]
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PubMed id
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Abstract
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PDZ domains are protein-protein interaction modules that generally bind to the C
termini of their target proteins. The C-terminal four amino acids of a
prospective binding partner of a PDZ domain are typically the determinants of
binding specificity. In an effort to determine the structures of a number of PDZ
domains we have included appropriate four residue extensions on the C termini of
PDZ domain truncation mutants, designed for self-binding. Multiple truncations
of each PDZ domain were generated. The four residue extensions, which represent
known specificity sequences of the target PDZ domains and cover both class I and
II motifs, form intermolecular contacts in the expected manner for the
interactions of PDZ domains with protein C termini for both classes. We present
the structures of eight unique PDZ domains crystallized using this approach and
focus on four which provide information on selectivity (PICK1 and the third PDZ
domain of DLG2), binding site flexibility (the third PDZ domain of MPDZ), and
peptide-domain interactions (MPDZ 12th PDZ domain). Analysis of our results
shows a clear improvement in the chances of obtaining PDZ domain crystals by
using this approach compared to similar truncations of the PDZ domains without
the C-terminal four residue extensions.
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Figure 2.
Figure 2. Ribbon diagrams of each of the 10 crystal forms (eight unique PDZ domains). The C-terminal four residues representing the PDZ recognition
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Figure 6.
Figure 6. Crystal structure of MPDZ@3. (A) Superimposition of the structures of MPDZ@3 and MPDZ@7 showing the opposite
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2007,
16,
683-694)
copyright 2007.
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