2KXS
ZO1 ZU5 domain in complex with GRINL1A peptide
2KXS の概要
| エントリーDOI | 10.2210/pdb2kxs/pdb |
| 関連するPDBエントリー | 2kxr |
| 分子名称 | Tight junction protein ZO-1,Myocardial zonula adherens protein (1 entity in total) |
| 機能のキーワード | beta-barrel, protein binding |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15540.85 |
| 構造登録者 | |
| 主引用文献 | Huo, L.,Wen, W.,Wang, R.,Kam, C.,Xia, J.,Feng, W.,Zhang, M. Cdc42-dependent formation of the ZO-1/MRCKb complex at the leading edge controls cell migration Embo J., 30:665-678, 2011 Cited by PubMed Abstract: Zonula occludens (ZO)-1 is a multi-domain scaffold protein known to have critical roles in the establishment of cell-cell adhesions and the maintenance of stable tissue structures through the targeting, anchoring, and clustering of transmembrane adhesion molecules and cytoskeletal proteins. Here, we report that ZO-1 directly binds to MRCKβ, a Cdc42 effector kinase that modulates cell protrusion and migration, at the leading edge of migrating cells. Structural studies reveal that the binding of a β hairpin from GRINL1A converts ZO-1 ZU5 into a complete ZU5-fold. A similar interaction mode is likely to occur between ZO-1 ZU5 and MRCKβ. The interaction between ZO-1 and MRCKβ requires the kinase to be primed by Cdc42 due to the closed conformation of the kinase. Formation of the ZO-1/MRCKβ complex enriches the kinase at the lamellae of migrating cells. Disruption of the ZO-1/MRCKβ complex inhibits MRCKβ-mediated cell migration. These results demonstrate that ZO-1, a classical scaffold protein with accepted roles in maintaining cell-cell adhesions in stable tissues, also has an active role in cell migration during processes such as tissue development and remodelling. PubMed: 21240187DOI: 10.1038/emboj.2010.353 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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