1ulc: Difference between revisions
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<StructureSection load='1ulc' size='340' side='right' caption='[[1ulc]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1ulc' size='340' side='right' caption='[[1ulc]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ulc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ulc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Copci Copci]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ULC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sla|1sla]], [[1qmj|1qmj]], [[1gan|1gan]], [[1c1f|1c1f]], [[1bkz|1bkz]], [[1a3k|1a3k]], [[1lcl|1lcl]], [[1is5|1is5]], [[1ul9|1ul9]], [[1uld|1uld]], [[1ule|1ule]], [[1ulf|1ulf]], [[1ulg|1ulg]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sla|1sla]], [[1qmj|1qmj]], [[1gan|1gan]], [[1c1f|1c1f]], [[1bkz|1bkz]], [[1a3k|1a3k]], [[1lcl|1lcl]], [[1is5|1is5]], [[1ul9|1ul9]], [[1uld|1uld]], [[1ule|1ule]], [[1ulf|1ulf]], [[1ulg|1ulg]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cgl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5346 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cgl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5346 COPCI])</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=1ulc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ulc RCSB], [http://www.ebi.ac.uk/pdbsum/1ulc PDBsum]</span></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=1ulc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulc OCA], [http://pdbe.org/1ulc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ulc RCSB], [http://www.ebi.ac.uk/pdbsum/1ulc PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1ulc" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Copci]] | ||
[[Category: Aebi, M]] | [[Category: Aebi, M]] | ||
[[Category: Ban, N]] | [[Category: Ban, N]] | ||
Revision as of 23:36, 9 September 2015
CGL2 in complex with lactoseCGL2 in complex with lactose
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRecognition 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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