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[[Image:1ulc.jpg|left|200px]]
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{{STRUCTURE_1ulc|  PDB=1ulc  |  SCENE=  }}
'''CGL2 in complex with lactose'''


==CGL2 in complex with lactose==
<StructureSection load='1ulc' size='340' side='right'caption='[[1ulc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ulc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULC 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]] 2.6&#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=1ulc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulc OCA], [https://pdbe.org/1ulc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ulc RCSB], [https://www.ebi.ac.uk/pdbsum/1ulc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CGL2_COPCI CGL2_COPCI] Binds lactose. May play a role in fruiting body formation.<ref>PMID:8999822</ref>
== 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/ul/1ulc_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=1ulc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Recognition of and discrimination between potential glyco-substrates is central to the function of galectins. Here we dissect the fundamental parameters responsible for such selectivity by the fungal representative, CGL2. The 2.1 A crystal structure of CGL2 and five substrate complexes reveal that this prototype galectin achieves increased substrate specificity by accommodating substituted oligosaccharides of the mammalian blood group A/B type in an extended binding cleft. Kinetic studies on wild-type and mutant CGL2 proteins demonstrate that the tetrameric organization is essential for functionality. The geometric constraints due to the orthogonal orientation of the four binding sites have important consequences on substrate binding and selectivity.


==Overview==
Structure and functional analysis of the fungal galectin CGL2.,Walser PJ, Haebel PW, Kunzler M, Sargent D, Kues U, Aebi M, Ban N Structure. 2004 Apr;12(4):689-702. PMID:15062091<ref>PMID:15062091</ref>
Recognition of and discrimination between potential glyco-substrates is central to the function of galectins. Here we dissect the fundamental parameters responsible for such selectivity by the fungal representative, CGL2. The 2.1 A crystal structure of CGL2 and five substrate complexes reveal that this prototype galectin achieves increased substrate specificity by accommodating substituted oligosaccharides of the mammalian blood group A/B type in an extended binding cleft. Kinetic studies on wild-type and mutant CGL2 proteins demonstrate that the tetrameric organization is essential for functionality. The geometric constraints due to the orthogonal orientation of the four binding sites have important consequences on substrate binding and selectivity.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1ULC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULC OCA].
</div>
<div class="pdbe-citations 1ulc" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure and functional analysis of the fungal galectin CGL2., Walser PJ, Haebel PW, Kunzler M, Sargent D, Kues U, Aebi M, Ban N, Structure. 2004 Apr;12(4):689-702. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15062091 15062091]
*[[Galectin 3D structures|Galectin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Coprinopsis cinerea]]
[[Category: Coprinopsis cinerea]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Aebi, M.]]
[[Category: Aebi M]]
[[Category: Ban, N.]]
[[Category: Ban N]]
[[Category: Haebel, P W.]]
[[Category: Haebel PW]]
[[Category: Kuenzler, M.]]
[[Category: Kuenzler M]]
[[Category: Kues, U.]]
[[Category: Kues U]]
[[Category: Walser, P J.]]
[[Category: Walser PJ]]
[[Category: Beta-galactoside binding lectin]]
[[Category: Galectin]]
[[Category: Lectin]]
[[Category: Sugar binding]]
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