2DFK
Crystal structure of the CDC42-Collybistin II complex
2DFK の概要
| エントリーDOI | 10.2210/pdb2dfk/pdb |
| 関連するPDBエントリー | 1DBH 1FOE 1KI1 1KZ7 1KZG 1LB1 |
| 分子名称 | collybistin II, cell division cycle 42 isoform 1, GLYCEROL, ... (5 entities in total) |
| 機能のキーワード | dh domain, ph domain, cell cycle |
| 由来する生物種 | Rattus norvegicus (Norway rat) 詳細 |
| 細胞内の位置 | Cytoplasm: Q9QX73 Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P60953 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 140386.29 |
| 構造登録者 | Xiang, S.,Kim, E.Y.,Connelly, J.J.,Nassar, N.,Kirsch, J.,Winking, J.,Schwarz, G.,Schindelin, H. (登録日: 2006-03-02, 公開日: 2006-05-02, 最終更新日: 2024-10-30) |
| 主引用文献 | Xiang, S.,Kim, E.Y.,Connelly, J.J.,Nassar, N.,Kirsch, J.,Winking, J.,Schwarz, G.,Schindelin, H. The Crystal Structure of Cdc42 in Complex with Collybistin II, a Gephyrin-interacting Guanine Nucleotide Exchange Factor. J.Mol.Biol., 359:35-46, 2006 Cited by PubMed Abstract: The synaptic localization of ion channel receptors is essential for efficient synaptic transmission and the precise regulation of diverse neuronal functions. In the central nervous system, ion channel receptors reside in the postsynaptic membrane where they are juxtaposed to presynaptic terminals. For proper function, these ion channels have to be anchored to the cytoskeleton, and in the case of the inhibitory glycine and gamma-amino-butyric acid type A (GABA(A)) receptors this interaction is mediated by a gephyrin centered scaffold. Highlighting its central role in this receptor anchoring scaffold, gephyrin interacts with a number of proteins, including the neurospecific guanine nucleotide exchange factor collybistin. Collybistin belongs to the Dbl family of guanine nucleotide exchange factors, occurs in multiple splice variants, and is specific for Cdc42, a small GTPase belonging to the Rho family. The 2.3 Angstroms resolution crystal structure of the Cdc42-collybistin II complex reveals a novel conformation of the switch I region of Cdc42. It also provides the first direct observation of structural changes in the relative orientation of the Dbl-homology domain and the pleckstrin-homology domain in the same Dbl family protein. Biochemical data indicate that gephyrin negatively regulates collybistin activity. PubMed: 16616186DOI: 10.1016/j.jmb.2006.03.019 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.15 Å) |
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