2ds0: Difference between revisions
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==Crystal structure of the earthworm lectin C-terminal domain mutant in complex with 6'-sialyllactose== | ==Crystal structure of the earthworm lectin C-terminal domain mutant in complex with 6'-sialyllactose== | ||
<StructureSection load='2ds0' size='340' side='right' caption='[[2ds0]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2ds0' size='340' side='right' caption='[[2ds0]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ds0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_earthworm Common earthworm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DS0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DS0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ds0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_earthworm Common earthworm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DS0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DS0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ao3|2ao3]], [[2d12|2d12]], [[2dry|2dry]], [[2drz|2drz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ao3|2ao3]], [[2d12|2d12]], [[2dry|2dry]], [[2drz|2drz]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ds0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ds0 OCA], [http://pdbe.org/2ds0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ds0 RCSB], [http://www.ebi.ac.uk/pdbsum/2ds0 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ds0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ds0 OCA], [http://pdbe.org/2ds0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ds0 RCSB], [http://www.ebi.ac.uk/pdbsum/2ds0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ds0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 09:20, 30 May 2018
Crystal structure of the earthworm lectin C-terminal domain mutant in complex with 6'-sialyllactoseCrystal structure of the earthworm lectin C-terminal domain mutant in complex with 6'-sialyllactose
Structural highlights
Publication Abstract from PubMedSialic 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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