1ulf

<table><tr><td colspan='2'>[[1ulf]] 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=1ULF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ULF FirstGlance]. <br>

</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=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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"><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]], [[1ulc|1ulc]], [[1uld|1uld]], [[1ule|1ule]], [[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 Agaricus cinereus])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ulf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulf OCA], [http://pdbe.org/1ulf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ulf RCSB], [http://www.ebi.ac.uk/pdbsum/1ulf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulf ProSAT]</span></td></tr>

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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ulf" style="background-color:#fffaf0;"></div>

[[Category: Agaricus cinereus]]

[[Category: Aebi, M]]

[[Category: Ban, N]]

[[Category: Haebel, P W]]

[[Category: Kuenzler, M]]

[[Category: Kues, U]]

[[Category: Walser, P J]]

[[Category: Sugar binding protein]]