1KTM
SOLUTION STRUCTURE OF FAT DOMAIN OF FOCAL ADHESION KINASE
Summary for 1KTM
| Entry DOI | 10.2210/pdb1ktm/pdb |
| NMR Information | BMRB: 5266,5677 |
| Descriptor | FOCAL ADHESION KINASE 1 (1 entity in total) |
| Functional Keywords | focal adhesion kinase, fak, focal adhension targeting domain, fat, helix bundle, transferase |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Cell junction, focal adhesion: Q00944 |
| Total number of polymer chains | 1 |
| Total formula weight | 15545.10 |
| Authors | Liu, G.,Guibao, C.,Zheng, J. (deposition date: 2002-01-16, release date: 2003-01-16, Last modification date: 2024-05-22) |
| Primary citation | Liu, G.,Guibao, C.,Zheng, J. Structural Insight into the Mechanisms of Targeting and Signaling of Focal Adhesion Kinase Mol.Cell.Biol., 22:2751-2760, 2002 Cited by PubMed Abstract: Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase whose focal adhesion targeting (FAT) domain interacts with other focal adhesion molecules in integrin-mediated signaling. Localization of activated FAK to focal adhesions is indispensable for its function. Here we describe a solution structure of the FAT domain bound to a peptide derived from paxillin, a FAK-binding partner. The FAT domain is composed of four helices that form a "right-turn" elongated bundle; the globular fold is mainly maintained by hydrophobic interactions. The bound peptide further stabilizes the structure. Certain signaling events such as phosphorylation and molecule interplay may induce opening of the helix bundle. Such conformational change is proposed to precede departure of FAK from focal adhesions, which starts focal adhesion turnover. PubMed: 11909967DOI: 10.1128/MCB.22.8.2751-2760.2002 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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