4tqj

</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=4tqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tqj OCA], [https://pdbe.org/4tqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tqj RCSB], [https://www.ebi.ac.uk/pdbsum/4tqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tqj ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

O-linked N-acetylglucosaminylation (O-GlcNAcylation) is a reversible post-translational modification that plays essential roles in many cellular pathways. Research in this field, however, is hampered by the lack of suitable probes to identify, accumulate, and purify the O-GlcNAcylated proteins. We have previously reported the identification of a lectin from the mushroom Agrocybe aegerita, i.e., Agrocybe aegerita lectin 2, or AAL2, that could bind terminal N-acetylglucosamine with higher affinities and specificity than other currently used probes. In this paper, we report the crystal structures of AAL2 and its complexes with GlcNAc and GlcNAcbeta1-3Galbeta1-4GlcNAc and reveal the structural basis of GlcNAc recognition by AAL2 and residues essential for the binding of terminal N-acetylglucosamine. Study on AAL2 may enable us to design a protein probe that can be used to identify and purify O-GlcNAcylated proteins more efficiently.

Structural Basis of Specific Recognition of Non-Reducing Terminal N-Acetylglucosamine by an Agrocybe aegerita Lectin.,Ren XM, Li DF, Jiang S, Lan XQ, Hu Y, Sun H, Wang DC PLoS One. 2015 Jun 26;10(6):e0129608. doi: 10.1371/journal.pone.0129608., eCollection 2015. PMID:26114302<ref>PMID:26114302</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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