1q47: Difference between revisions

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New page: left|200px<br /><applet load="1q47" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q47, resolution 2.8Å" /> '''Structure of the Sema...
 
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[[Image:1q47.gif|left|200px]]<br /><applet load="1q47" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1q47.gif|left|200px]]<br /><applet load="1q47" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1q47, resolution 2.8&Aring;" />
caption="1q47, resolution 2.8&Aring;" />
'''Structure of the Semaphorin 3A Receptor-Binding Module'''<br />
'''Structure of the Semaphorin 3A Receptor-Binding Module'''<br />


==Overview==
==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.
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==
==About this Structure==
1Q47 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q47 OCA].  
1Q47 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q47 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Antipenko, A.]]
[[Category: Antipenko, A.]]
[[Category: Barton, W.A.]]
[[Category: Barton, W A.]]
[[Category: Himanen, J-P.]]
[[Category: Himanen, J-P.]]
[[Category: Hoemme, C.]]
[[Category: Hoemme, C.]]
[[Category: Lesniak, J.]]
[[Category: Lesniak, J.]]
[[Category: Leyen, K.van.]]
[[Category: Leyen, K van.]]
[[Category: Lu, M.]]
[[Category: Lu, M.]]
[[Category: Nardi-Dei, V.]]
[[Category: Nardi-Dei, V.]]
[[Category: Nikolov, D.]]
[[Category: Nikolov, D.]]
[[Category: Puschel, A.]]
[[Category: Puschel, A.]]
[[Category: Rajashankar, K.R.]]
[[Category: Rajashankar, K R.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: beta propeller]]
[[Category: beta propeller]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:22:24 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:45 2008''

Revision as of 15:35, 21 February 2008

File:1q47.gif


1q47, resolution 2.8Å

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Structure of the Semaphorin 3A Receptor-Binding Module

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 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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