2drz
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(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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Revision as of 17:10, 29 January 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 (Tokyo). 2007 Jan 18;. PMID:17234683
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