First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
3f6q
From Proteopedia
| 3f6q, resolution 1.60Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , , , , , , , and | ||||||||
| Ligands: | , , | ||||||||
| Gene: | ILK, ILK1, ILK2 (Homo sapiens), LIMS1, PINCH, PINCH1 (Homo sapiens) | ||||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal structure of integrin-linked kinase ankyrin repeat domain in complex with PINCH1 LIM1 domain
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.
The structural basis of integrin-linked kinase-PINCH interactions., Chiswell BP, Zhang R, Murphy JW, Boggon TJ, Calderwood DA, Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):20677-82. Epub 2008 Dec 12. PMID:19074270
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3F6Q is a 2 chains structure with sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Chiswell BP, Zhang R, Murphy JW, Boggon TJ, Calderwood DA. The structural basis of integrin-linked kinase-PINCH interactions. Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):20677-82. Epub 2008 Dec 12. PMID:19074270 doi:0811415106
Page seeded by OCA on Wed Sep 22 11:47:15 2010
Categories: Homo sapiens | Non-specific serine/threonine protein kinase | Boggon, T J. | Calderwood, D A. | Chiswell, B P. | Acetylation | Ank | Ank repeat | Ankyrin repeat | Atp-binding | Cell junction | Cell membrane | Ilk | Integrin-linked kinase | Integrin-mediated signaling | Ipp | Kinase | Lim | Lim domain | Membrane | Metal-binding | Nucleotide-binding | Phosphoprotein | Pinch | Serine/threonine-protein kinase | Signaling protein/signaling protein complex | Transferase | Transferase/metal binding protein complex | Zinc
