1ulf: Difference between revisions
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[[Image:1ulf.jpg|left|200px]] | [[Image:1ulf.jpg|left|200px]] | ||
'''CGL2 in complex with Blood Group A tetrasaccharide''' | {{Structure | ||
|PDB= 1ulf |SIZE=350|CAPTION= <scene name='initialview01'>1ulf</scene>, resolution 2.36Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= cgl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5346 Coprinopsis cinerea]) | |||
}} | |||
'''CGL2 in complex with Blood Group A tetrasaccharide''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ULF is a [ | 1ULF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULF OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15062091 15062091] | ||
[[Category: Coprinopsis cinerea]] | [[Category: Coprinopsis cinerea]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sugar binding]] | [[Category: sugar binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:33:33 2008'' | ||
Revision as of 15:33, 20 March 2008
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| , resolution 2.36Å | |||||||
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| Gene: | cgl2 (Coprinopsis cinerea) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CGL2 in complex with Blood Group A tetrasaccharide
OverviewOverview
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 StructureAbout this Structure
1ULF is a Single protein structure of sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Mar 20 14:33:33 2008