1q47: Difference between revisions

Revision as of 14:39, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1q47.png

Template:STRUCTURE 1q47

Structure of the Semaphorin 3A Receptor-Binding ModuleStructure of the Semaphorin 3A Receptor-Binding Module

Template:ABSTRACT PUBMED 12925274

About this StructureAbout this Structure

1Q47 is a Single protein structure of sequence from Mus musculus. 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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OCA

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-==Overview==
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-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.
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 [[Category: Rajashankar, K R.]]
 [[Category: Beta propeller]]
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