6fx3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 6fx3 is ON HOLD  until Paper Publication
==crystal structure of Pholiota squarrosa lectin in complex with a dodecasaccharide==
<StructureSection load='6fx3' size='340' side='right' caption='[[6fx3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fx3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FX3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=C4W:1-azido-beta-N-acetyl-D-glucosamine'>C4W</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></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=6fx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fx3 OCA], [http://pdbe.org/6fx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fx3 RCSB], [http://www.ebi.ac.uk/pdbsum/6fx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fx3 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We recombinantly produced and characterized the mini fungal lectin PhoSL. Despite a length of only 40 amino acids, PhoSL exclusively recognizes N-glycans with beta1,6-linked fucose. Core fucosylation influences the intrinsic properties and bioactivities of mammalian N-glycoproteins and its level is linked to various cancers. Thus, PhoSL serves as a promising tool for glycoprofiling. Without structural precedence, we solved its crystal structure using the zinc anomalous signal. We revealed an interlaced trimer creating a novel protein fold termed beta-prism III. Three biantennary core fucosylated N-glycan azides of 8 to 12 sugars were cocrystallized with PhoSL. The resulting highly resolved structures gave a detailed view on how the exclusive recognition of alpha1,6-fucosylated N-glycans by such a small protein occurs. This work also provided a protein consensus motif for the observed specificity as well as a glimpse on N-glycan flexibility upon binding.


Authors: Cabanettes, A., Varrot, A.
Recognition of complex core fucosylated N-glycans by a mini lectin.,Cabanettes A, Perkams L, Spies C, Unverzagt C, Varrot A Angew Chem Int Ed Engl. 2018 Jun 29. doi: 10.1002/anie.201805165. PMID:29956878<ref>PMID:29956878</ref>


Description: crystal structure of Pholiota squarrosa lectin in complex with a dodecasaccharide
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6fx3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cabanettes, A]]
[[Category: Cabanettes, A]]
[[Category: Varrot, A]]
[[Category: Varrot, A]]
[[Category: Dodecasaccharide]]
[[Category: Lectin]]
[[Category: Sugar binding protein]]