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[[Image:1lem.gif|left|200px]]


{{Structure
==THE MONOSACCHARIDE BINDING SITE OF LENTIL LECTIN: AN X-RAY AND MOLECULAR MODELLING STUDY==
|PDB= 1lem |SIZE=350|CAPTION= <scene name='initialview01'>1lem</scene>, resolution 3.0&Aring;
<StructureSection load='1lem' size='340' side='right'caption='[[1lem]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
<table><tr><td colspan='2'>[[1lem]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LEM FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
|GENE=
<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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1lem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lem OCA], [https://pdbe.org/1lem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lem RCSB], [https://www.ebi.ac.uk/pdbsum/1lem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lem ProSAT]</span></td></tr>
 
</table>
'''THE MONOSACCHARIDE BINDING SITE OF LENTIL LECTIN: AN X-RAY AND MOLECULAR MODELLING STUDY'''
== Function ==
 
[https://www.uniprot.org/uniprot/LEC_LENCU LEC_LENCU] D-mannose specific lectin (By similarity).
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
The X-ray crystal structure of lentil lectin in complex with alpha-D-glucopyranose has been determined by molecular replacement and refined to an R-value of 0.20 at 3.0 A resolution. The glucose interacts with the protein in a manner similar to that found in the mannose complexes of concanavalin A, pea lectin and isolectin I from Lathyrus ochrus. The complex is stabilized by a network of hydrogen bonds involving the carbohydrate oxygens O6, O4, O3 and O5. In addition, the alpha-D-glucopyranose residue makes van der Waals contacts with the protein, involving the phenyl ring of Phe123 beta. The overall structure of lentil lectin, at this resolution, does not differ significantly from the highly refined structures of the uncomplexed lectin. Molecular docking studies were performed with mannose and its 2-O and 3-O-m-nitro-benzyl derivatives to explain their high affinity binding. The interactions of the modelled mannose with lentil lectin agree well with those observed experimentally for the protein-carbohydrate complex. The highly flexible Me-2-O-(m-nitro-benzyl)-alpha-D-mannopyranoside and Me-3-O-(m-nitro-benzyl)-alpha-D-mannopyranoside become conformationally restricted upon binding to lentil lectin. For best orientations of the two substrates in the combining site, the loss of entropy is accompanied by the formation of a strong hydrogen bond between the nitro group and one amino acid, Gly97 beta and Asn125 beta, respectively, along with the establishment of van der Waals interactions between the benzyl group and the aromatic amino acids Tyr100 beta and Trp128 beta.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/le/1lem_consurf.spt"</scriptWhenChecked>
1LEM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEM OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
The monosaccharide binding site of lentil lectin: an X-ray and molecular modelling study., Loris R, Casset F, Bouckaert J, Pletinckx J, Dao-Thi MH, Poortmans F, Imberty A, Perez S, Wyns L, Glycoconj J. 1994 Dec;11(6):507-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7696853 7696853]
</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=1lem ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lens culinaris]]
[[Category: Lens culinaris]]
[[Category: Protein complex]]
[[Category: Loris R]]
[[Category: Loris, R.]]
[[Category: Wyns L]]
[[Category: Wyns, L.]]
[[Category: CA]]
[[Category: GLC]]
[[Category: MN]]
[[Category: lectin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:30:02 2008''

Latest revision as of 07:32, 14 February 2024

THE MONOSACCHARIDE BINDING SITE OF LENTIL LECTIN: AN X-RAY AND MOLECULAR MODELLING STUDY

1lem, resolution 3.00Å

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