View source for 1tei


==STRUCTURE OF CONCANAVALIN A COMPLEXED TO BETA-D-GLCNAC (1,2)ALPHA-D-MAN-(1,6)[BETA-D-GLCNAC(1,2)ALPHA-D-MAN (1,6)]ALPHA-D-MAN==
<StructureSection load='1tei' size='340' side='right'caption='[[1tei]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tei]] 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=1TEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TEI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <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=1tei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tei OCA], [https://pdbe.org/1tei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tei RCSB], [https://www.ebi.ac.uk/pdbsum/1tei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tei ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
== 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/te/1tei_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=1tei ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Carbohydrate recognition by proteins is a key event in many biological processes. Concanavalin A is known to specifically recognize the pentasaccharide core (beta-GlcNAc-(1--&gt;2)-alpha- Man-(1--&gt;3)-[beta-GlcNAc-(1--&gt;2)-alpha-Man-(1--&gt;6)]-Man) of N-linked oligosaccharides with a Ka of 1.41 x 10(6 )M-1. We have determined the structure of concanavalin A bound to beta-GlcNAc-(1--&gt;2)-alpha-Man-(1--&gt;3)-[beta-GlcNAc-(1--&gt;2)-alpha-Man- (1--&gt;6)]-Man to 2.7A. In six of eight subunits there is clear density for all five sugar residues and a well ordered binding site. The pentasaccharide adopts the same conformation in all eight subunits. The binding site is a continuous extended cleft on the surface of the protein. Van der Waals interactions and hydrogen bonds anchor the carbohydrate to the protein. Both GlcNAc residues contact the protein. The GlcNAc on the 1--&gt;6 arm of the pentasaccharide makes particularly extensive contacts and including two hydrogen bonds. The binding site of the 1--&gt;3 arm GlcNAc is much less extensive. Oligosaccharide recognition by Con A occurs through specific protein carbohydrate interactions and does not require recruitment of adventitious water molecules. The beta-GlcNAc-(1--&gt;2)-Man glycosidic linkage PSI torsion angle on the 1--&gt;6 arm is rotated by over 50 degrees from that observed in solution. This rotation is coupled to disruption of interactions at the monosaccharide site. We suggest destabilization of the monosaccharide site and the conformational strain reduces the free energy liberated by additional interactions at the 1--&gt;6 arm GlcNAc site.

Concanavalin A distorts the beta-GlcNAc-(1--&gt;2)-Man linkage of beta-GlcNAc-(1--&gt;2)-alpha-Man-(1--&gt;3)-[beta-GlcNAc-(1--&gt;2)-alpha-Man- (1--&gt;6)]-Man upon binding.,Moothoo DN, Naismith JH Glycobiology. 1998 Feb;8(2):173-81. PMID:9451027<ref>PMID:9451027</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tei" style="background-color:#fffaf0;"></div>

==See Also==
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Canavalia ensiformis]]
[[Category: Large Structures]]
[[Category: Moothoo DN]]
[[Category: Naismith JH]]