1Q47

Structure of the Semaphorin 3A Receptor-Binding Module

Summary for 1Q47

• Entry DOI: 10.2210/pdb1q47/pdb
• Descriptor: Semaphorin 3A, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: beta propeller, signaling protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Secreted: O08665
• Total number of polymer chains: 2
• Total formula weight: 113812.00

Authors

Antipenko, A.,Himanen, J.-P.,van Leyen, K.,Nardi-Dei, V.,Lesniak, J.,Barton, W.A.,Rajashankar, K.R.,Lu, M.,Hoemme, C.,Puschel, A.,Nikolov, D. (deposition date: 2003-08-01, release date: 2004-08-03, Last modification date: 2024-11-06)

Primary citation

Antipenko, A.,Himanen, J.-P.,van Leyen, K.,Nardi-Dei, V.,Lesniak, J.,Barton, W.A.,Rajashankar, K.R.,Lu, M.,Hoemme, C.,Puschel, A.W.,Nikolov, D.B.
Structure of the semaphorin-3A receptor binding module.
Neuron, 39:589-598, 2003

PubMed Abstract: The semaphorins are a large group of extracellular proteins involved in a variety of processes during development, including neuronal migration and axon guidance. Their distinctive feature is a conserved 500 amino acid semaphorin domain, a ligand-receptor interaction module also present in plexins and scatter-factor receptors. We report the crystal structure of a secreted 65 kDa form of Semaphorin-3A (Sema3A), containing the full semaphorin domain. Unexpectedly, the semaphorin fold is a variation of the beta propeller topology. Analysis of the Sema3A structure and structure-based mutagenesis data identify the neuropilin binding site and suggest a potential plexin interaction site. Based on the structure, we present a model for the initiation of semaphorin signaling and discuss potential similarities with the signaling mechanisms of other beta propeller cell surface receptors, such as integrins and the LDL receptor.

PubMed: 12925274
DOI: 10.1016/S0896-6273(03)00502-6

Experimental method

X-RAY DIFFRACTION (2.8 Å)