1ulc
From Proteopedia
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|PDB= 1ulc |SIZE=350|CAPTION= <scene name='initialview01'>1ulc</scene>, resolution 2.60Å | |PDB= 1ulc |SIZE=350|CAPTION= <scene name='initialview01'>1ulc</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= cgl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5346 Coprinopsis cinerea]) | |GENE= cgl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5346 Coprinopsis cinerea]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[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]] | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1ulc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ulc RCSB]</span> | ||
}} | }} | ||
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[[Category: sugar binding]] | [[Category: sugar binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:11:52 2008'' |
Revision as of 21:11, 30 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | cgl2 (Coprinopsis cinerea) | ||||||
| Related: | 1SLA, 1QMJ, 1GAN, 1C1F, 1BKZ, 1A3K, 1LCL, 1IS5, 1UL9, 1ULD, 1ULE, 1ULF, 1ULG
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CGL2 in complex with lactose
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
1ULC 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
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