4tqj
From Proteopedia
(Difference between revisions)
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<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=4tqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tqj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tqj RCSB], [http://www.ebi.ac.uk/pdbsum/4tqj 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=4tqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tqj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tqj RCSB], [http://www.ebi.ac.uk/pdbsum/4tqj PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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[[Category: Glcnac]] | [[Category: Glcnac]] | ||
[[Category: Lectin]] | [[Category: Lectin]] | ||
| + | [[Category: Sugar binding protein]] | ||
Revision as of 13:45, 5 August 2015
Structural basis of specific recognition of non-reducing terminal N-acetylglucosamine by an Agrocybe aegerita lection
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