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2drz
From Proteopedia
(New page: 200px<br /><applet load="2drz" size="350" color="white" frame="true" align="right" spinBox="true" caption="2drz, resolution 2.19Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Sialic acid (Sia) is a typical terminal sugar, which modifies various | + | 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== | ==About this Structure== | ||
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==Reference== | ==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 ( | + | 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: Lumbricus terrestris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sugar complex]] | [[Category: sugar complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:57 2008'' |
Revision as of 15:01, 21 February 2008
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Crystal structure of the earthworm lectin C-terminal domain mutant in complex with lactose
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.
About this Structure
2DRZ is a Single protein structure of sequence from Lumbricus terrestris with as ligand. Full crystallographic information is available from OCA.
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. 2007 Mar;141(3):389-99. Epub 2007 Jan 18. PMID:17234683
Page seeded by OCA on Thu Feb 21 17:01:57 2008
