1U6H
Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)
1U6H の概要
エントリーDOI | 10.2210/pdb1u6h/pdb |
分子名称 | Vinculin, Talin (3 entities in total) |
機能のキーワード | protein-protein complex, cell adhesion |
由来する生物種 | Gallus gallus (chicken) 詳細 |
細胞内の位置 | Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P12003 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 34460.74 |
構造登録者 | Fillingham, I.,Gingras, A.R.,Papagrigoriou, E.,Patel, B.,Emsley, J.,Roberts, G.C.K.,Critchley, D.R.,Barsukov, I.L. (登録日: 2004-07-30, 公開日: 2005-01-18, 最終更新日: 2024-04-03) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.38 Å) |
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