[SEM3A_MOUSE] Plays a role in growth cones guidance. May function to pattern sensory projections by selectively repelling axons that normally terminate dorsally.
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Structure of the semaphorin-3A receptor binding module.,Antipenko A, Himanen JP, van Leyen K, Nardi-Dei V, Lesniak J, Barton WA, Rajashankar KR, Lu M, Hoemme C, Puschel AW, Nikolov DB Neuron. 2003 Aug 14;39(4):589-98. PMID:12925274[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Antipenko A, Himanen JP, van Leyen K, Nardi-Dei V, Lesniak J, Barton WA, Rajashankar KR, Lu M, Hoemme C, Puschel AW, Nikolov DB. Structure of the semaphorin-3A receptor binding module. Neuron. 2003 Aug 14;39(4):589-98. PMID:12925274
