1ulc

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(New page: 200px<br /><applet load="1ulc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ulc, resolution 2.60&Aring;" /> '''CGL2 in complex with...)
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[[Image:1ulc.jpg|left|200px]]<br /><applet load="1ulc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ulc, resolution 2.60&Aring;" />
 
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'''CGL2 in complex with lactose'''<br />
 
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==Overview==
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==CGL2 in complex with lactose==
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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.
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<StructureSection load='1ulc' size='340' side='right'caption='[[1ulc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.6&#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=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>
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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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CGL2_COPCI CGL2_COPCI] Binds lactose. May play a role in fruiting body formation.<ref>PMID:8999822</ref>
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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/ul/1ulc_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=1ulc 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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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.
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==About this Structure==
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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>
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1ULC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ULC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15062091 15062091]
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</div>
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[[Category: Coprinopsis cinerea]]
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<div class="pdbe-citations 1ulc" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Aebi, M.]]
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[[Category: Ban, N.]]
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[[Category: Haebel, P.W.]]
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[[Category: Kuenzler, M.]]
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[[Category: Kues, U.]]
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[[Category: Walser, P.J.]]
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[[Category: beta-galactoside binding lectin]]
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[[Category: galectin]]
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[[Category: lectin]]
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[[Category: sugar binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:13:13 2007''
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==See Also==
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*[[Galectin 3D structures|Galectin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Coprinopsis cinerea]]
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[[Category: Large Structures]]
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[[Category: Aebi M]]
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[[Category: Ban N]]
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[[Category: Haebel PW]]
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[[Category: Kuenzler M]]
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[[Category: Kues U]]
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[[Category: Walser PJ]]

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CGL2 in complex with lactose

PDB ID 1ulc

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