1ulc: Difference between revisions
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==CGL2 in complex with lactose== | ==CGL2 in complex with lactose== | ||
<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/Agaricus_cinereus Agaricus cinereus]. 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://proteopedia.org/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" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[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]]</div></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 Agaricus cinereus])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Galectin|Galectin]] | *[[Galectin 3D structures|Galectin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Agaricus cinereus]] | ||
[[Category: Large Structures]] | |||
[[Category: Aebi, M]] | [[Category: Aebi, M]] | ||
[[Category: Ban, N]] | [[Category: Ban, N]] | ||
Revision as of 10:29, 30 December 2020
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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