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==Crystal structure of the earthworm lectin C-terminal domain mutant in complex with lactose== | |||
<StructureSection load='2drz' size='340' side='right'caption='[[2drz]], [[Resolution|resolution]] 2.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2drz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lumbricus_terrestris Lumbricus terrestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DRZ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2drz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2drz OCA], [https://pdbe.org/2drz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2drz RCSB], [https://www.ebi.ac.uk/pdbsum/2drz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2drz ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O96048_LUMTE O96048_LUMTE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:17234683</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2drz" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Galactose-binding lectin|Galactose-binding lectin]] | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Lumbricus terrestris]] | [[Category: Lumbricus terrestris]] | ||
[[Category: Fujimoto Z]] | |||
[[Category: Fujimoto | [[Category: Suzuki R]] | ||
[[Category: Suzuki | |||
Latest revision as of 13:35, 16 August 2023
Crystal structure of the earthworm lectin C-terminal domain mutant in complex with lactoseCrystal structure of the earthworm lectin C-terminal domain mutant in complex with lactose
Structural highlights
FunctionPublication 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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