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4M8N

Crystal Structure of PlexinC1/Rap1B Complex

Summary for 4M8N
Entry DOI10.2210/pdb4m8n/pdb
DescriptorPlexinC1 Intracellular Region, Ras-related protein Rap-1b, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordsgtpase, gtpase activating protein, rap, gtp binding, magnesium binding, membrane, signaling protein
Biological sourceDanio rerio (leopard danio,zebra danio,zebra fish)
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Cellular locationCell membrane: P61224
Total number of polymer chains8
Total formula weight364709.50
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 citationWang, 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: 24137545
DOI: 10.7554/eLife.01279
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.294 Å)
Structure validation

238268

数据于2025-07-02公开中

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