1q47: Difference between revisions

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 <StructureSection load='1q47' size='340' side='right'caption='[[1q47]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1q47]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1Q47 FirstGlance]. <br>
+<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]] 2.8&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q47 OCA], [http://pdbe.org/1q47 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q47 RCSB], [http://www.ebi.ac.uk/pdbsum/1q47 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q47 ProSAT]</span></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>
+<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>
 == Function ==
-[[http://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.
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </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="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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1q47" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Semaphorin|Semaphorin]]
+*[[Semaphorin 3D structures|Semaphorin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Antipenko, A]]
+[[Category: Antipenko A]]
-[[Category: Barton, W A]]
+[[Category: Barton WA]]
-[[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: 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 KR]]
-[[Category: Rajashankar, K R]]
+[[Category: Van Leyen K]]
-[[Category: Beta propeller]]
-[[Category: Signaling protein]]