2ds0: Difference between revisions

Revision as of 18:02, 21 February 2008

Crystal structure of the earthworm lectin C-terminal domain mutant in complex with 6'-sialyllactose

OverviewOverview

Sialic acid (Sia) is a typical terminal sugar, which modifies various types of glycoconjugates commonly found in higher animals. Its regulatory roles in diverse biological phenomena are frequently triggered by interaction with Sia-binding lectins. When using natural Sia-binding lectins as probes, however, there have been practical problems concerning their repertoire and availability. Here, we show a rational creation of a Sia-binding lectin based on the strategy 'natural evolution-mimicry', where Sia-binding lectins are engineered by error-prone PCR from a Gal-binding lectin used as a scaffold protein. After selection with fetuin-agarose using a recently reinforced ribosome display system, one of the evolved mutants SRC showed substantial affinity for alpha2-6Sia, which the parental Gal-binding lectin EW29Ch lacked. SRC was found to have additional practical advantages in productivity and in preservation of affinity for Gal. Thus, the developed novel Sia-recognition protein will contribute as useful tools to sialoglycomics.

About this StructureAbout this Structure

2DS0 is a Single protein structure of sequence from Lumbricus terrestris with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry., Yabe R, Suzuki R, Kuno A, Fujimoto Z, Jigami Y, Hirabayashi J, J Biochem. 2007 Mar;141(3):389-99. Epub 2007 Jan 18. PMID:17234683

Page seeded by OCA on Thu Feb 21 17:02:01 2008

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OCA

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 ==Overview==
-Sialic acid (Sia) is a typical terminal sugar, which modifies various, types of glycoconjugates commonly found in higher animals. Its regulatory, roles in diverse biological phenomena are frequently triggered by, interaction with Sia-binding lectins. When using natural Sia-binding, lectins as probes, however, there have been practical problems concerning, their repertoire and availability. Here, we show a rational creation of a, Sia-binding lectin based on the strategy "natural evolution-mimicry", where Sia-binding lectins are engineered by error-prone PCR from a, Gal-binding lectin used as a scaffold protein. After selection with, fetuin-agarose using a recently reinforced ribosome display system, one of, the evolved mutants SRC showed substantial affinity for alpha2-6Sia, which, the parental Gal-binding lectin EW29Ch lacked. SRC was found to have, additional practical advantages in productivity and in preservation of, affinity for Gal. Thus, the developed novel Sia-recognition protein will, contribute as useful tools to sialoglycomics.
+Sialic acid (Sia) is a typical terminal sugar, which modifies various types of glycoconjugates commonly found in higher animals. Its regulatory roles in diverse biological phenomena are frequently triggered by interaction with Sia-binding lectins. When using natural Sia-binding lectins as probes, however, there have been practical problems concerning their repertoire and availability. Here, we show a rational creation of a Sia-binding lectin based on the strategy 'natural evolution-mimicry', where Sia-binding lectins are engineered by error-prone PCR from a Gal-binding lectin used as a scaffold protein. After selection with fetuin-agarose using a recently reinforced ribosome display system, one of the evolved mutants SRC showed substantial affinity for alpha2-6Sia, which the parental Gal-binding lectin EW29Ch lacked. SRC was found to have additional practical advantages in productivity and in preservation of affinity for Gal. Thus, the developed novel Sia-recognition protein will contribute as useful tools to sialoglycomics.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry., Yabe R, Suzuki R, Kuno A, Fujimoto Z, Jigami Y, Hirabayashi J, J Biochem (Tokyo). 2007 Jan 18;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17234683 17234683]
+Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry., Yabe R, Suzuki R, Kuno A, Fujimoto Z, Jigami Y, Hirabayashi J, J Biochem. 2007 Mar;141(3):389-99. Epub 2007 Jan 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17234683 17234683]
 [[Category: Lumbricus terrestris]]
 [[Category: Single protein]]
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 [[Category: sugar complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:10:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:01 2008''