2DFK
Crystal structure of the CDC42-Collybistin II complex
Summary for 2DFK
| Entry DOI | 10.2210/pdb2dfk/pdb |
| Related | 1DBH 1FOE 1KI1 1KZ7 1KZG 1LB1 |
| Descriptor | collybistin II, cell division cycle 42 isoform 1, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | dh domain, ph domain, cell cycle |
| Biological source | Rattus norvegicus (Norway rat) More |
| Cellular location | Cytoplasm: Q9QX73 Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P60953 |
| Total number of polymer chains | 4 |
| Total formula weight | 140386.29 |
| Authors | Xiang, S.,Kim, E.Y.,Connelly, J.J.,Nassar, N.,Kirsch, J.,Winking, J.,Schwarz, G.,Schindelin, H. (deposition date: 2006-03-02, release date: 2006-05-02, Last modification date: 2024-10-30) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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