View source for 2rst


==NMR structure of the C-terminal domain of EW29==
<StructureSection load='2rst' size='340' side='right'caption='[[2rst]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rst]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lumbricus_terrestris Lumbricus terrestris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RST FirstGlance]. <br>
</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=2rst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rst OCA], [https://pdbe.org/2rst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rst RCSB], [https://www.ebi.ac.uk/pdbsum/2rst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rst ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O96048_LUMTE O96048_LUMTE] 
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== Publication Abstract from PubMed ==
The C-terminal domain (Ch; C-half) of the R-type earthworm 29-kDa lectin (EW29), isolated from the earthworm Lumbricus terrestris, has two sugar-binding sites, in subdomains alpha and gamma, and the protein uses the two sugar-binding sites for its function as a single domain-type haemagglutinin. Our previous NMR titration experiments showed that the alpha sugar-binding site is a high-affinity site and the gamma sugar-binding site is a low-affinity site. However, it remains unclear why the alpha sugar-binding site of EW29Ch binds to lactose much more strongly because the crystal structure of lactose-bound EW29Ch showed that the interaction between the alpha sugar-binding site and lactose was almost same as that between the gamma sugar-binding site and lactose. In the present study, we have determined the NMR structure of EW29Ch in the sugar-free state and performed (15)N relaxation experiments for EW29Ch in both the sugar-free state and the lactose-bound states. The conformation of EW29Ch in the sugar-free state was similar to that of EW29Ch in complex with lactose. Conformational changes upon binding of lactose were observed only for the alpha sugar-binding site. By contrast, the (15)N relaxation experiments revealed a conformational exchange at the alpha sugar-binding site in the sugar-free state, which was suppressed in the lactose-bound state. The conformational exchange phenomenon observed for the alpha sugar-binding site was not observed for the gamma sugar-binding site. Differences in the conformational change and the backbone dynamics between subdomains alpha and gamma may be associated with the difference of the sugar-binding modes between the two sugar-binding sites. DATABASE: Structural data for the NMR structure of EW29Ch in the sugar-free state have been deposited in the Protein Data Bank database under accession number 2RST.

NMR structure and dynamics of the C-terminal domain of R-type lectin from the earthworm Lumbricus terrestris.,Hemmi H, Kuno A, Hirabayashi J FEBS J. 2013 Jan;280(1):70-82. doi: 10.1111/febs.12050. Epub 2012 Nov 23. PMID:23122331<ref>PMID:23122331</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2rst" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galactose-binding lectin|Galactose-binding lectin]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Lumbricus terrestris]]
[[Category: Hemmi H]]