1ul9

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[[Image:1ul9.gif|left|200px]]
[[Image:1ul9.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ul9 |SIZE=350|CAPTION= <scene name='initialview01'>1ul9</scene>, resolution 2.22&Aring;
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The line below this paragraph, containing "STRUCTURE_1ul9", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= cgl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5346 Coprinopsis cinerea])
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|DOMAIN=
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{{STRUCTURE_1ul9| PDB=1ul9 | SCENE= }}
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|RELATEDENTRY=[[1sla|1SLA]], [[1qmj|1QMJ]], [[1gan|1GAN]], [[1c1f|1C1F]], [[1bkz|1BKZ]], [[1a3k|1A3K]], [[1lcl|1LCL]], [[1is5|1IS5]], [[1ulc|1ULC]], [[1uld|1ULD]], [[1ule|1ULE]], [[1ulf|1ULF]], [[1ulg|1ULG]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ul9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ul9 OCA], [http://www.ebi.ac.uk/pdbsum/1ul9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ul9 RCSB]</span>
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}}
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'''CGL2 ligandfree'''
'''CGL2 ligandfree'''
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[[Category: Kues, U.]]
[[Category: Kues, U.]]
[[Category: Walser, P J.]]
[[Category: Walser, P J.]]
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[[Category: beta-galactoside binding lectin]]
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[[Category: Beta-galactoside binding lectin]]
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[[Category: galectin]]
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[[Category: Galectin]]
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[[Category: lectin]]
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[[Category: Lectin]]
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[[Category: sugar binding]]
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[[Category: Sugar binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:22:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:11:47 2008''
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Revision as of 08:22, 3 May 2008

Image:1ul9.gif

Template:STRUCTURE 1ul9

CGL2 ligandfree


Overview

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

1UL9 is a Single protein structure of sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 11:22:48 2008

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