1vln: Difference between revisions

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-{{Seed}}
-[[Image:1vln.png|left|200px]]
-<!--
+==A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A==
-The line below this paragraph, containing "STRUCTURE_1vln", creates the "Structure Box" on the page.
+<StructureSection load='1vln' size='340' side='right'caption='[[1vln]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1vln]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLN FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-{{STRUCTURE_1vln|  PDB=1vln  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vln OCA], [https://pdbe.org/1vln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vln RCSB], [https://www.ebi.ac.uk/pdbsum/1vln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vln ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LECA_DIOGR LECA_DIOGR] D-mannose/D-glucose-binding lectin. Has anti-inflammatory activity in rats. Induces histamine release in mast cells from rat. Induces lymphocyte proliferation and IFNG production. Shows toxicity against the aquatic snail B.glabrata at concentrations higher than 50 ug/ml.<ref>PMID:1398779</ref> <ref>PMID:7524287</ref> <ref>PMID:18472821</ref> <ref>PMID:9575151</ref> <ref>PMID:10747944</ref> <ref>PMID:19765980</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vl/1vln_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1vln ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The molecular structure of a triclinic crystal form of concanavalin A has been refined at 2.4 A resolution. The crystals have unit cell dimensions a = 78.8 A, b = 79.3 A, c = 133.3 A, alpha = 97.1degrees, beta = 90.2degrees, and gamma = 97.5degrees and contain two tetramers per asymmetric unit each with approximate 222 symmetry. The final crystallographic R-factor is 0.205 and the free-R-factor is 0.265 in the resolution range 6.0 to 2.4 A. The conformation of the tetramer is more similar to that found in concanavalin A saccharide complexes than in the previously reported I222 crystal form of uncomplexed concanavalin A. A comparison of the molecular packing between the two crystal forms shows a more open arrangement with large solvent channels through the crystal.
-===A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A===
+A Triclinic Crystal Form of the Lectin Concanavalin A,Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ J Struct Biol. 1996 Jul;117(1):16-23. PMID:8812975<ref>PMID:8812975</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1vln" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_8812975}}, adds the Publication Abstract to the page
+*[[Concanavalin 3D structures|Concanavalin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 8812975 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8812975}}
+__TOC__
+</StructureSection>
-==About this Structure==
-VLN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLN OCA].
-==Reference==
-A Triclinic Crystal Form of the Lectin Concanavalin A, Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ, J Struct Biol. 1996 Jul;117(1):16-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8812975 8812975]
 [[Category: Canavalia ensiformis]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Hamodrakas, S J.]]
+[[Category: Hamodrakas SJ]]
-[[Category: Kanellopoulos, P N.]]
+[[Category: Kanellopoulos PN]]
-[[Category: Tucker, P A.]]
+[[Category: Tucker PA]]
-[[Category: Calcium]]
-[[Category: Lectin]]
-[[Category: Legume]]
-[[Category: Manganese]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:08:13 2008''