4M8N
Crystal Structure of PlexinC1/Rap1B Complex
Summary for 4M8N
Entry DOI | 10.2210/pdb4m8n/pdb |
Descriptor | PlexinC1 Intracellular Region, Ras-related protein Rap-1b, MAGNESIUM ION, ... (6 entities in total) |
Functional Keywords | gtpase, gtpase activating protein, rap, gtp binding, magnesium binding, membrane, signaling protein |
Biological source | Danio rerio (leopard danio,zebra danio,zebra fish) More |
Cellular location | Cell membrane: P61224 |
Total number of polymer chains | 8 |
Total formula weight | 364709.50 |
Authors | Pascoe, H.G.,Wang, Y.,Brautigam, C.A.,He, H.,Zhang, X. (deposition date: 2013-08-13, release date: 2013-10-09, Last modification date: 2024-02-28) |
Primary citation | Wang, Y.,Pascoe, H.G.,Brautigam, C.A.,He, H.,Zhang, X. Structural basis for activation and non-canonical catalysis of the Rap GTPase activating protein domain of plexin. Elife, 2:e01279-e01279, 2013 Cited by PubMed Abstract: Plexins are cell surface receptors that bind semaphorins and transduce signals for regulating neuronal axon guidance and other processes. Plexin signaling depends on their cytoplasmic GTPase activating protein (GAP) domain, which specifically inactivates the Ras homolog Rap through an ill-defined non-canonical catalytic mechanism. The plexin GAP is activated by semaphorin-induced dimerization, the structural basis for which remained unknown. Here we present the crystal structures of the active dimer of zebrafish PlexinC1 cytoplasmic region in the apo state and in complex with Rap. The structures show that the dimerization induces a large-scale conformational change in plexin, which opens the GAP active site to allow Rap binding. Plexin stabilizes the switch II region of Rap in an unprecedented conformation, bringing Gln63 in Rap into the active site for catalyzing GTP hydrolysis. The structures also explain the unique Rap-specificity of plexins. Mutational analyses support that these mechanisms underlie plexin activation and signaling. DOI:http://dx.doi.org/10.7554/eLife.01279.001. PubMed: 24137545DOI: 10.7554/eLife.01279 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.294 Å) |
Structure validation
Download full validation report
