View source for 2dry


==Crystal structure of the earthworm lectin C-terminal domain mutant==
<StructureSection load='2dry' size='340' side='right'caption='[[2dry]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dry]] 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=2DRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DRY 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=2dry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dry OCA], [https://pdbe.org/2dry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dry RCSB], [https://www.ebi.ac.uk/pdbsum/2dry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dry 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2dry" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galactose-binding lectin|Galactose-binding lectin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lumbricus terrestris]]
[[Category: Fujimoto Z]]
[[Category: Suzuki R]]