1q47

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[[Image:1q47.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q47 OCA], [http://www.ebi.ac.uk/pdbsum/1q47 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q47 RCSB]</span>
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'''Structure of the Semaphorin 3A Receptor-Binding Module'''
'''Structure of the Semaphorin 3A Receptor-Binding Module'''
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[[Category: Puschel, A.]]
[[Category: Puschel, A.]]
[[Category: Rajashankar, K R.]]
[[Category: Rajashankar, K R.]]
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[[Category: beta propeller]]
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[[Category: Beta propeller]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:50:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:08:38 2008''
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Revision as of 02:50, 3 May 2008

Template:STRUCTURE 1q47

Structure of the Semaphorin 3A Receptor-Binding Module


Overview

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 Structure

1Q47 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 05:50:58 2008

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