3F6Q
Crystal structure of integrin-linked kinase ankyrin repeat domain in complex with PINCH1 LIM1 domain
Summary for 3F6Q
| Entry DOI | 10.2210/pdb3f6q/pdb |
| Descriptor | Integrin-linked protein kinase, LIM and senescent cell antigen-like-containing domain protein 1, IODIDE ION, ... (6 entities in total) |
| Functional Keywords | ilk, integrin-linked kinase, pinch, lim, ankyrin repeat, ank, ipp, integrin-mediated signaling, ank repeat, atp-binding, cell junction, cell membrane, kinase, membrane, nucleotide-binding, phosphoprotein, serine/threonine-protein kinase, transferase, acetylation, lim domain, metal-binding, zinc, transferase-metal binding protein complex, signaling protein-signaling protein complex, signaling protein/signaling protein |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Cell junction, focal adhesion: Q13418 P48059 |
| Total number of polymer chains | 2 |
| Total formula weight | 31055.14 |
| Authors | Chiswell, B.P.,Calderwood, D.A.,Boggon, T.J. (deposition date: 2008-11-06, release date: 2008-12-02, Last modification date: 2023-09-06) |
| Primary citation | Chiswell, B.P.,Zhang, R.,Murphy, J.W.,Boggon, T.J.,Calderwood, D.A. The structural basis of integrin-linked kinase-PINCH interactions. Proc.Natl.Acad.Sci.USA, 105:20677-20682, 2008 Cited by PubMed Abstract: The heterotrimeric complex between integrin-linked kinase (ILK), PINCH, and parvin is an essential signaling platform, serving as a convergence point for integrin and growth-factor signaling and regulating cell adhesion, spreading, and migration. We report a 1.6-A crystal structure of the ILK ankyrin repeat domain bound to the PINCH1 LIM1 domain, revealing the molecular basis of ILK-PINCH interactions and providing a structural description of this region of ILK. This structure identifies 5 ankyrin repeats in ILK, explains previous deletion mutagenesis data, permits identification of ILK and PINCH1 point mutations that disrupt the interaction, shows how zincs are coordinated by PINCH1 LIM1, and suggests that conformational flexibility and twisting between the 2 zinc fingers within the LIM1 domain may be important for ILK binding. These data provide an atomic-resolution description of a key interaction in the ILK-PINCH-parvin scaffolding complex. PubMed: 19074270DOI: 10.1073/pnas.0811415106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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