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==Pterocarpus angolensis Lectin (PAL) In Complex With D-Mannose (anomeric mixture)== | |||
<StructureSection load='2are' size='340' side='right'caption='[[2are]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2are]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pterocarpus_angolensis Pterocarpus angolensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ARE 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=2are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2are OCA], [https://pdbe.org/2are PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2are RCSB], [https://www.ebi.ac.uk/pdbsum/2are PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2are ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8GSD2_PTEAG Q8GSD2_PTEAG] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ar/2are_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2are ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of Pterocarpus angolensis lectin is determined in its ligand-free state, in complex with the fucosylated biantennary complex type decasaccharide NA2F, and in complex with a series of smaller oligosaccharide constituents of NA2F. These results together with thermodynamic binding data indicate that the complete oligosaccharide binding site of the lectin consists of five subsites allowing the specific recognition of the pentasaccharide GlcNAc beta(1-2)Man alpha(1-3)[GlcNAc beta(1-2)Man alpha(1-6)]Man. The mannose on the 1-6 arm occupies the monosaccharide binding site while the GlcNAc residue on this arm occupies a subsite that is almost identical to that of concanavalin A (con A). The core mannose and the GlcNAc beta(1-2)Man moiety on the 1-3 arm on the other hand occupy a series of subsites distinct from those of con A. | |||
Structural basis for the recognition of complex-type biantennary oligosaccharides by Pterocarpus angolensis lectin.,Buts L, Garcia-Pino A, Imberty A, Amiot N, Boons GJ, Beeckmans S, Versees W, Wyns L, Loris R FEBS J. 2006 Jun;273(11):2407-20. PMID:16704415<ref>PMID:16704415</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2are" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Pal|Pal]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pterocarpus angolensis]] | [[Category: Pterocarpus angolensis]] | ||
[[Category: Amiot N]] | |||
[[Category: Amiot | [[Category: Beeckmans S]] | ||
[[Category: Beeckmans | [[Category: Boons G-J]] | ||
[[Category: Boons | [[Category: Buts L]] | ||
[[Category: Buts | [[Category: Garcia-Pino A]] | ||
[[Category: Garcia-Pino | [[Category: Imberty A]] | ||
[[Category: Imberty | [[Category: Lah J]] | ||
[[Category: Lah | [[Category: Loris R]] | ||
[[Category: Loris | [[Category: Versees W]] | ||
[[Category: Versees | [[Category: Wyns L]] | ||
[[Category: Wyns | |||
Latest revision as of 10:28, 23 August 2023
Pterocarpus angolensis Lectin (PAL) In Complex With D-Mannose (anomeric mixture)Pterocarpus angolensis Lectin (PAL) In Complex With D-Mannose (anomeric mixture)
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of Pterocarpus angolensis lectin is determined in its ligand-free state, in complex with the fucosylated biantennary complex type decasaccharide NA2F, and in complex with a series of smaller oligosaccharide constituents of NA2F. These results together with thermodynamic binding data indicate that the complete oligosaccharide binding site of the lectin consists of five subsites allowing the specific recognition of the pentasaccharide GlcNAc beta(1-2)Man alpha(1-3)[GlcNAc beta(1-2)Man alpha(1-6)]Man. The mannose on the 1-6 arm occupies the monosaccharide binding site while the GlcNAc residue on this arm occupies a subsite that is almost identical to that of concanavalin A (con A). The core mannose and the GlcNAc beta(1-2)Man moiety on the 1-3 arm on the other hand occupy a series of subsites distinct from those of con A. Structural basis for the recognition of complex-type biantennary oligosaccharides by Pterocarpus angolensis lectin.,Buts L, Garcia-Pino A, Imberty A, Amiot N, Boons GJ, Beeckmans S, Versees W, Wyns L, Loris R FEBS J. 2006 Jun;273(11):2407-20. PMID:16704415[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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