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1cvn

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[[Image:1cvn.gif|left|200px]]
 
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==CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE==
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The line below this paragraph, containing "STRUCTURE_1cvn", creates the "Structure Box" on the page.
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<StructureSection load='1cvn' size='340' side='right'caption='[[1cvn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1cvn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. The April 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Concanavalin A and Circular Permutation'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_4 10.2210/rcsb_pdb/mom_2010_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CVN FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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></td></tr>
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{{STRUCTURE_1cvn| PDB=1cvn | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvn OCA], [https://pdbe.org/1cvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cvn RCSB], [https://www.ebi.ac.uk/pdbsum/1cvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cvn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/1cvn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1cvn ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Despite the fact that complex saccharides play an important role in many biological recognition processes, molecular level descriptions of protein-carbohydrate interactions are sparse. The legume lectin concanavalin A (con A), from Canavalia ensiformis, specifically recognizes the trimannoside core of many complex glycans. We have determined the crystal structure of a con A-trimannoside complex at 2.3-A resolution now describe the trimannoside interaction with conA. All three sugar residues are in well defined difference electron density. The 1,6-linked mannose residue is bound at the previously reported monosaccharide binding site; the other two sugars bind in an extended cleft formed by residues Tyr-12, Pro-13, Asn-14, Thr-15, and Asp-16. Hydrogen bonds are formed between the protein and all three sugar residues. In particular, the 1,3-linked mannose residue makes a strong hydrogen bond with the main chain of the protein. In addition, a water molecule, which is conserved in other con A structures, plays an important role in anchoring the reducing sugar unit to the protein. The complex is further stabilized by van der Waals interactions. The structure provides a rationale for the high affinity of con A for N-linked glycans.
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'''CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE'''
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Structural basis of trimannoside recognition by concanavalin A.,Naismith JH, Field RA J Biol Chem. 1996 Jan 12;271(2):972-6. PMID:8557713<ref>PMID:8557713</ref>
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==Overview==
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Despite the fact that complex saccharides play an important role in many biological recognition processes, molecular level descriptions of protein-carbohydrate interactions are sparse. The legume lectin concanavalin A (con A), from Canavalia ensiformis, specifically recognizes the trimannoside core of many complex glycans. We have determined the crystal structure of a con A-trimannoside complex at 2.3-A resolution now describe the trimannoside interaction with conA. All three sugar residues are in well defined difference electron density. The 1,6-linked mannose residue is bound at the previously reported monosaccharide binding site; the other two sugars bind in an extended cleft formed by residues Tyr-12, Pro-13, Asn-14, Thr-15, and Asp-16. Hydrogen bonds are formed between the protein and all three sugar residues. In particular, the 1,3-linked mannose residue makes a strong hydrogen bond with the main chain of the protein. In addition, a water molecule, which is conserved in other con A structures, plays an important role in anchoring the reducing sugar unit to the protein. The complex is further stabilized by van der Waals interactions. The structure provides a rationale for the high affinity of con A for N-linked glycans.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1CVN 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=1CVN OCA].
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</div>
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<div class="pdbe-citations 1cvn" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structural basis of trimannoside recognition by concanavalin A., Naismith JH, Field RA, J Biol Chem. 1996 Jan 12;271(2):972-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8557713 8557713]
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*[[Concanavalin 3D structures|Concanavalin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
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[[Category: Single protein]]
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[[Category: Concanavalin A and Circular Permutation]]
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[[Category: Naismith, J H.]]
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[[Category: Large Structures]]
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[[Category: Concanavalin some]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Saccharide binding]]
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[[Category: Naismith JH]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:09:40 2008''
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CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE

PDB ID 1cvn

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