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3SU8

Crystal structure of a truncated intracellular domain of Plexin-B1 in complex with Rac1

Summary for 3SU8
Entry DOI10.2210/pdb3su8/pdb
Related3SUA
DescriptorRas-related C3 botulinum toxin substrate 1, Plexin-B1, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsaxon guidance, signal transduction, apoptosis-signaling protein complex, apoptosis/signaling protein
Biological sourceHomo sapiens (human)
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Cellular locationIsoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted: P63000
Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity): O43157
Total number of polymer chains2
Total formula weight91076.09
Authors
Bell, C.H.,Aricescu, A.R.,Jones, E.Y.,Siebold, C. (deposition date: 2011-07-11, release date: 2011-09-28, Last modification date: 2024-02-28)
Primary citationBell, C.H.,Aricescu, A.R.,Jones, E.Y.,Siebold, C.
A Dual Binding Mode for RhoGTPases in Plexin Signalling.
Plos Biol., 9:e1001134-e1001134, 2011
Cited by
PubMed Abstract: Plexins are cell surface receptors for the semaphorin family of cell guidance cues. The cytoplasmic region comprises a Ras GTPase-activating protein (GAP) domain and a RhoGTPase binding domain. Concomitant binding of extracellular semaphorin and intracellular RhoGTPase triggers GAP activity and signal transduction. The mechanism of this intricate regulation remains elusive. We present two crystal structures of the human Plexin-B1 cytoplasmic region in complex with a constitutively active RhoGTPase, Rac1. The structure of truncated Plexin-B1-Rac1 complex provides no mechanism for coupling RhoGTPase and Ras binding sites. On inclusion of the juxtamembrane helix, a trimeric structure of Plexin-B1-Rac1 complexes is stabilised by a second, novel, RhoGTPase binding site adjacent to the Ras site. Site-directed mutagenesis combined with cellular and biophysical assays demonstrate that this new binding site is essential for signalling. Our findings are consistent with a model in which extracellular and intracellular plexin clustering events combine into a single signalling output.
PubMed: 21912513
DOI: 10.1371/journal.pbio.1001134
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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数据于2024-10-30公开中

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