4XEV
Fusion of Pyk2-FAT domain with Leupaxin LD1 motif, complexed with Leupaxin LD4 peptide
Summary for 4XEV
| Entry DOI | 10.2210/pdb4xev/pdb |
| Related | 4XEF 4XEK |
| Descriptor | Fusion protein of Protein-tyrosine kinase 2-beta FAT domain and Leupaxin LD1 motif, 19-mer peptide containing Leupaxin LD4 motif (3 entities in total) |
| Functional Keywords | 4-helix bundle, focal adhesion, tyrosine kinase, leupaxin, cell adhesion |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 40249.63 |
| Authors | Miller, D.J. (deposition date: 2014-12-24, release date: 2015-12-30, Last modification date: 2023-09-27) |
| Primary citation | Vanarotti, M.S.,Finkelstein, D.B.,Guibao, C.D.,Nourse, A.,Miller, D.J.,Zheng, J.J. Structural Basis for the Interaction between Pyk2-FAT Domain and Leupaxin LD Repeats. Biochemistry, 55:1332-1345, 2016 Cited by PubMed Abstract: 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. PubMed: 26866573DOI: 10.1021/acs.biochem.5b01274 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.0073 Å) |
Structure validation
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