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New page: left|200px<br /> <applet load="1hlc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hlc, resolution 2.9Å" /> '''X-RAY CRYSTAL STRUCT...
 
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[[Image:1hlc.gif|left|200px]]<br />
<applet load="1hlc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hlc, resolution 2.9&Aring;" />
'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION'''<br />


==Overview==
==X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION==
S-Lac lectins are a family of soluble lactose-binding animal lectins, some, of which have been implicated in modulating cell-cell and cell-matrix, interactions through specific carbohydrate-mediated recognition. We report, here the x-ray crystal structure of a representative member of this, family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two, extended anti-parallel beta-sheets, which associate in a beta-sandwich, motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant, lectins, suggesting a conserved structure-function relationship., Carbohydrate binding by L-14-II was found to involve protein residues that, are very highly conserved among all S-Lac lectins. These residues map to a, single DNA exon, suggesting a carbohydrate binding cassette common to all, S-Lac lectins.
<StructureSection load='1hlc' size='340' side='right'caption='[[1hlc]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hlc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HLC 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</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=1hlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlc OCA], [https://pdbe.org/1hlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hlc RCSB], [https://www.ebi.ac.uk/pdbsum/1hlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hlc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LEG2_HUMAN LEG2_HUMAN] This protein binds beta-galactoside. Its physiological function is not yet known.
== 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/hl/1hlc_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=1hlc ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known disease associated with this structure: Myocardial infarction, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=150571 150571]]
*[[Galectin 3D structures|Galectin 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
1HLC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HLC OCA].
 
==Reference==
X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution., Lobsanov YD, Gitt MA, Leffler H, Barondes SH, Rini JM, J Biol Chem. 1993 Dec 25;268(36):27034-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8262940 8262940]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Barondes, S.]]
[[Category: Barondes S]]
[[Category: Gitt, M.A.]]
[[Category: Gitt MA]]
[[Category: Leffler, H.]]
[[Category: Leffler H]]
[[Category: Lobsanov, Y.D.]]
[[Category: Lobsanov YD]]
[[Category: Rini, J.M.]]
[[Category: Rini JM]]
[[Category: lectin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:19:45 2007''

Latest revision as of 07:28, 7 February 2024

X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION

1hlc, resolution 2.90Å

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