1U89
Solution structure of VBS2 fragment of talin
Summary for 1U89
| Entry DOI | 10.2210/pdb1u89/pdb |
| Related | 1SJ7 1SJ8 |
| NMR Information | BMRB: 6285 |
| Descriptor | Talin 1 (1 entity in total) |
| Functional Keywords | 4-helix bundle, left-handed, structural protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26039 |
| Total number of polymer chains | 1 |
| Total formula weight | 14396.91 |
| Authors | Fillingham, I.,Gingras, A.R.,Papagrigoriou, E.,Patel, B.,Emsley, J.,Roberts, G.C.K.,Critchley, D.R.,Barsukov, I.L. (deposition date: 2004-08-05, release date: 2005-01-18, Last modification date: 2024-05-29) |
| Primary citation | Fillingham, I.,Gingras, A.R.,Papagrigoriou, E.,Patel, B.,Emsley, J.,Critchley, D.R.,Roberts, G.C.,Barsukov, I.L. A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head. Structure, 13:65-74, 2005 Cited by PubMed Abstract: The cytoskeletal protein talin plays a key role in activating integrins and in coupling them to the actin cytoskeleton. Its N-terminal globular head, which binds beta integrins, is linked to an extended rod having a C-terminal actin binding site and several vinculin binding sites (VBSs). The NMR structure of residues 755-889 of the rod (containing a VBS) is shown to be an amphipathic four-helix bundle with a left-handed topology. A talin peptide corresponding to the VBS binds the vinculin head; the X-ray crystallographic structure of this complex shows that the residues which interact with vinculin are buried in the hydrophobic core of the talin fragment. NMR shows that the interaction involves a major structural change in the talin fragment, including unfolding of one of its helices, making the VBS accessible to vinculin. Interestingly, the talin 755-889 fragment binds more than one vinculin head molecule, suggesting that the talin rod may contain additional as yet unrecognized VBSs. PubMed: 15642262DOI: 10.1016/j.str.2004.11.006 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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