1q47
Structure of the Semaphorin 3A Receptor-Binding Module
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OverviewOverview
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.
About this StructureAbout this Structure
1Q47 is a Single protein structure of sequence from Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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