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PDBsum entry 4xek
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Cell adhesion
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PDB id
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4xek
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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 interaction between pyk2-Fat domain and leupaxin ld repeats.
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Authors
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M.S.Vanarotti,
D.B.Finkelstein,
C.D.Guibao,
A.Nourse,
D.J.Miller,
J.J.Zheng.
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Ref.
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Biochemistry, 2016,
55,
1332-1345.
[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 nonreceptor tyrosine kinase and
belongs to the focal adhesion kinase (FAK) family. Like FAK, the C-terminal
focal adhesion-targeting (FAT) domain of Pyk2 binds to paxillin, a scaffold
protein in focal adhesions; however, the interaction between the FAT domain of
Pyk2 and paxillin is dynamic and unstable. Leupaxin is another member in the
paxillin family and was suggested to be the native binding partner of Pyk2; Pyk2
gene expression is strongly correlated with that of leupaxin in many tissues
including primary breast cancer. Here, we report that leupaxin interacts with
Pyk2-FAT. Leupaxin has four leucine-aspartate (LD) motifs. The first and third
LD motifs of leupaxin preferably target the two LD-binding sites on the Pyk2-FAT
domain, respectively. Moreover, the full-length leupaxin binds to Pyk2-FAT as a
stable one-to-one complex. Together, we propose that there is an underlying
selectivity between leupaxin and paxillin for Pyk2, which may influence the
differing behavior of the two proteins at focal adhesion sites.
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