1ulc
From Proteopedia
(New page: 200px<br /><applet load="1ulc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ulc, resolution 2.60Å" /> '''CGL2 in complex with...) |
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| - | [[Image:1ulc.jpg|left|200px]]<br /><applet load="1ulc" size=" | + | [[Image:1ulc.jpg|left|200px]]<br /><applet load="1ulc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ulc, resolution 2.60Å" /> | caption="1ulc, resolution 2.60Å" /> | ||
'''CGL2 in complex with lactose'''<br /> | '''CGL2 in complex with lactose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Recognition of and discrimination between potential glyco-substrates is | + | 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== | ==About this Structure== | ||
| - | 1ULC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http:// | + | 1ULC is a [http://en.wikipedia.org/wiki/Single_protein 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=1ULC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Aebi, M.]] | [[Category: Aebi, M.]] | ||
[[Category: Ban, N.]] | [[Category: Ban, N.]] | ||
| - | [[Category: Haebel, P | + | [[Category: Haebel, P W.]] |
[[Category: Kuenzler, M.]] | [[Category: Kuenzler, M.]] | ||
[[Category: Kues, U.]] | [[Category: Kues, U.]] | ||
| - | [[Category: Walser, P | + | [[Category: Walser, P J.]] |
[[Category: beta-galactoside binding lectin]] | [[Category: beta-galactoside binding lectin]] | ||
[[Category: galectin]] | [[Category: galectin]] | ||
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[[Category: sugar binding]] | [[Category: sugar binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:54 2008'' |
Revision as of 13:25, 21 February 2008
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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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