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PDBsum entry 3u3f
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Transferase/signaling protein
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PDB id
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3u3f
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Contents |
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130 a.a.
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13 a.a.
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12 a.a.
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14 a.a.
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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 and mechanistic insights into the interaction between pyk2 and paxillin ld motifs.
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Authors
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M.S.Vanarotti,
D.J.Miller,
C.D.Guibao,
A.Nourse,
J.J.Zheng.
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Ref.
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J Mol Biol, 2014,
426,
3985-4001.
[DOI no: ]
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PubMed id
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Abstract
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Proline-rich tyrosine kinase 2 (Pyk2) is a member of the focal adhesion kinase
(FAK) subfamily of cytoplasmic tyrosine kinases. The C-terminal Pyk2-focal
adhesion targeting (FAT) domain binds to paxillin, an adhesion molecule.
Paxillin has five leucine-aspartate (LD) motifs (LD1-LD5). Here, we show that
the second LD motif of paxillin, LD2, interacts with Pyk2-FAT, similar to the
known Pyk2-FAT/LD4 interaction. Both LD motifs can target two ligand binding
sites on Pyk2-FAT. Interestingly, they also share similar binding affinity for
Pyk2-FAT with preferential association to one site relative to the other.
Nevertheless, the LD2-LD4 region of paxillin (paxillin(133-290)) binds to
Pyk2-FAT as a 1:1 complex. However, our data suggest that the Pyk2-FAT and
paxillin complex is dynamic and it appears to be a mixture of two distinct
conformations of paxillin that almost equally compete for Pyk2-FAT binding.
These studies provide insight into the underlying selectivity of paxillin for
Pyk2 and FAK that may influence the differing behavior of these two closely
related kinases in focal adhesion sites.
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