2cy6

<StructureSection load='2cy6' size='340' side='right' caption='[[2cy6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[2cy6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canavalia_rosea Canavalia rosea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CY6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cwm|2cwm]], [[2cyf|2cyf]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cy6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cy6 RCSB], [http://www.ebi.ac.uk/pdbsum/2cy6 PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/2cy6_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The crystal structure of Canavalia maritima lectin (ConM) complexed with trehalose and maltose revealed relevant point mutations in ConA-like lectins. ConM with the disaccharides and other ConA-like lectins complexed with carbohydrates demonstrated significant differences in the position of H-bonds. The main difference in the ConM structure is the replacement of Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to the carbohydrate-binding site. The O-6' of the second glucose ring in maltose interacts with Tyr12, while in trehalose the interaction is established by the O-2' and Tyr12, explaining the higher affinity of ConM for disaccharides compared to monosaccharides.

Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins.,Delatorre P, Rocha BA, Gadelha CA, Santi-Gadelha T, Cajazeiras JB, Souza EP, Nascimento KS, Freire VN, Sampaio AH, Azevedo WF Jr, Cavada BS J Struct Biol. 2006 Jun;154(3):280-6. Epub 2006 Apr 21. PMID:16677825<ref>PMID:16677825</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Concanavalin A|Concanavalin A]]

[[Category: Azevedo, W F]]

[[Category: Cavada, B S]]

[[Category: Delatorre, P]]

[[Category: Gadelha, C A.A]]

[[Category: Souza, E P]]

[[Category: Canavalia maritima]]

[[Category: Lectin]]

[[Category: Metal binding protein]]

[[Category: Trehalose]]