1qf3
From Proteopedia
(New page: 200px<br /><applet load="1qf3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qf3, resolution 2.80Å" /> '''PEANUT LECTIN COMPLE...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1qf3.jpg|left|200px]]<br /><applet load="1qf3" size=" | + | [[Image:1qf3.jpg|left|200px]]<br /><applet load="1qf3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qf3, resolution 2.80Å" /> | caption="1qf3, resolution 2.80Å" /> | ||
'''PEANUT LECTIN COMPLEXED WITH METHYL-BETA-GALACTOSE'''<br /> | '''PEANUT LECTIN COMPLEXED WITH METHYL-BETA-GALACTOSE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of complexes of peanut lectin with | + | The crystal structures of complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine have been determined at 2.8 and 2.7 A, respectively. These, and the complexes involving lactose and the T-antigenic disaccharide reported previously, permit a detailed characterization of peanut-lectin-carbohydrate association and the role of water molecules therein. The water molecules in the combining site are substantially conserved in the four complexes. The role of interacting sugar hydroxyl groups, when absent, are often mimicked by ordered water molecules not only at the primary combining site, but also at the site of the second sugar ring. The similarity of peanut-lectin-sugar interactions with those in other galactose/N-acetylgalactosamine-specific lectins also extend to a substantial degree to water bridges. The comparative study provides a structural explanation for the exclusive specificity of peanut lectin for galactose at the monosaccharide level, compared with that of the other lectins for galactose as well as N-acetylgalactosamine. The complexes also provide a qualitative structural rationale for differences in the strengths of binding of peanut lectin to different sugars. |
==About this Structure== | ==About this Structure== | ||
| - | 1QF3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea] with MBG, CA and MN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1QF3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea] with <scene name='pdbligand=MBG:'>MBG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QF3 OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 26: | ||
[[Category: water bridges]] | [[Category: water bridges]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:47 2008'' |
Revision as of 12:38, 21 February 2008
|
PEANUT LECTIN COMPLEXED WITH METHYL-BETA-GALACTOSE
Overview
The crystal structures of complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine have been determined at 2.8 and 2.7 A, respectively. These, and the complexes involving lactose and the T-antigenic disaccharide reported previously, permit a detailed characterization of peanut-lectin-carbohydrate association and the role of water molecules therein. The water molecules in the combining site are substantially conserved in the four complexes. The role of interacting sugar hydroxyl groups, when absent, are often mimicked by ordered water molecules not only at the primary combining site, but also at the site of the second sugar ring. The similarity of peanut-lectin-sugar interactions with those in other galactose/N-acetylgalactosamine-specific lectins also extend to a substantial degree to water bridges. The comparative study provides a structural explanation for the exclusive specificity of peanut lectin for galactose at the monosaccharide level, compared with that of the other lectins for galactose as well as N-acetylgalactosamine. The complexes also provide a qualitative structural rationale for differences in the strengths of binding of peanut lectin to different sugars.
About this Structure
1QF3 is a Single protein structure of sequence from Arachis hypogaea with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins., Ravishankar R, Suguna K, Surolia A, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1375-82. PMID:10417405
Page seeded by OCA on Thu Feb 21 14:38:47 2008
