1q47
From Proteopedia
(Difference between revisions)
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<StructureSection load='1q47' size='340' side='right'caption='[[1q47]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1q47' size='340' side='right'caption='[[1q47]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1q47]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1q47]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q47 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q47 OCA], [https://pdbe.org/1q47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q47 RCSB], [https://www.ebi.ac.uk/pdbsum/1q47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q47 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/SEM3A_MOUSE 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q47 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q47 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == 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<ref>PMID:12925274</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1q47" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
- | *[[Semaphorin|Semaphorin]] | + | *[[Semaphorin 3D structures|Semaphorin 3D structures]] |
- | + | ||
- | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: Antipenko | + | [[Category: Antipenko A]] |
- | [[Category: Barton | + | [[Category: Barton WA]] |
- | [[Category: Himanen | + | [[Category: Himanen J-P]] |
- | [[Category: Hoemme | + | [[Category: Hoemme C]] |
- | [[Category: Lesniak | + | [[Category: Lesniak J]] |
- | + | [[Category: Lu M]] | |
- | [[Category: Lu | + | [[Category: Nardi-Dei V]] |
- | [[Category: Nardi-Dei | + | [[Category: Nikolov D]] |
- | [[Category: Nikolov | + | [[Category: Puschel A]] |
- | [[Category: Puschel | + | [[Category: Rajashankar KR]] |
- | [[Category: Rajashankar | + | [[Category: Van Leyen K]] |
- | [[Category: | + | |
- | + |
Revision as of 06:01, 17 April 2024
Structure of the Semaphorin 3A Receptor-Binding Module
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Categories: Large Structures | Mus musculus | Antipenko A | Barton WA | Himanen J-P | Hoemme C | Lesniak J | Lu M | Nardi-Dei V | Nikolov D | Puschel A | Rajashankar KR | Van Leyen K