5FZT
The crystal structure of R7R8 in complex with a DLC1 fragment.
Summary for 5FZT
| Entry DOI | 10.2210/pdb5fzt/pdb |
| Descriptor | TALIN-1, RHO GTPASE-ACTIVATING PROTEIN 7, MALONATE ION, ... (4 entities in total) |
| Functional Keywords | structural protein, talin, dlc1, focal adhesion |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Cellular location | Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side : P26039 Cytoplasm: Q96QB1 |
| Total number of polymer chains | 2 |
| Total formula weight | 35582.01 |
| Authors | Zacharchenko, T.,Qian, X.,Goult, B.T.,Jethwa, D.,Almeida, T.,Ballestrem, C.,Critchley, D.R.,Lowy, D.R.,Barsukov, I.L. (deposition date: 2016-03-15, release date: 2016-04-27, Last modification date: 2024-01-10) |
| Primary citation | Zacharchenko, T.,Qian, X.,Goult, B.T.,Jethwa, D.,Almeida, T.B.,Ballestrem, C.,Critchley, D.R.,Lowy, D.R.,Barsukov, I.L. Ld Motif Recognition by Talin: Structure of the Talin-Dlc1 Complex. Structure, 24:1130-, 2016 Cited by PubMed Abstract: Cell migration requires coordination between integrin-mediated cell adhesion to the extracellular matrix and force applied to adhesion sites. Talin plays a key role in coupling integrin receptors to the actomyosin contractile machinery, while deleted in liver cancer 1 (DLC1) is a Rho GAP that binds talin and regulates Rho, and therefore actomyosin contractility. We show that the LD motif of DLC1 forms a helix that binds to the four-helix bundle of the talin R8 domain in a canonical triple-helix arrangement. We demonstrate that the same R8 surface interacts with the paxillin LD1 and LD2 motifs. We identify key charged residues that stabilize the R8 interactions with LD motifs and demonstrate their importance in vitro and in cells. Our results suggest a network of competitive interactions in adhesion complexes that involve LD motifs, and identify mutations that can be used to analyze the biological roles of specific protein-protein interactions in cell migration. PubMed: 27265849DOI: 10.1016/J.STR.2016.04.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
