1zgr: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1zgr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Parkia_platycephala Parkia platycephala]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZGR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1zgr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Parkia_platycephala Parkia platycephala]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZGR FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zgs|1zgs]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=1zgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zgr OCA], [https://pdbe.org/1zgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zgr RCSB], [https://www.ebi.ac.uk/pdbsum/1zgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zgr ProSAT]</span></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=1zgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zgr OCA], [https://pdbe.org/1zgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zgr RCSB], [https://www.ebi.ac.uk/pdbsum/1zgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zgr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/LEC_PARPC LEC_PARPC]] Mannose/glucose specific lectin. Shows agglutinating activity against rabbit erythrocytes.<ref>PMID:11502201</ref>
[https://www.uniprot.org/uniprot/LEC_PARPC LEC_PARPC] Mannose/glucose specific lectin. Shows agglutinating activity against rabbit erythrocytes.<ref>PMID:11502201</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1zgr ConSurf].
</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=1zgr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of the apo and mannose-bound Parkia platycephala seed lectin represent the first structure of a Mimosoideae lectin and a novel circular arrangement of beta-prism domains, and highlight the adaptability of the beta-prism fold as a building block in the evolution of plant lectins. The P.platycephala lectin is a dimer both in solution and in the crystals. Mannose binding to each of the three homologous carbohydrate-recognition domains of the lectin occurs through different modes, and restrains the flexibility of surface-exposed loops and residues involved in carbohydrate recognition. The planar array of carbohydrate-binding sites on the rim of the toroid-shaped structure of the P.platycephala lectin dimer immediately suggests a mechanism to promote multivalent interactions leading to cross-linking of carbohydrate ligands as part of the host strategy against phytopredators and pathogens. The cyclic structure of the P.platycephala lectin points to the convergent evolution of a structural principle for the construction of lectins involved in host defense or in attacking other organisms.
The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain.,Gallego del Sol F, Nagano C, Cavada BS, Calvete JJ J Mol Biol. 2005 Oct 28;353(3):574-83. Epub 2005 Sep 9. PMID:16185708<ref>PMID:16185708</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1zgr" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Parkia platycephala]]
[[Category: Parkia platycephala]]
[[Category: Calvete, J J]]
[[Category: Calvete JJ]]
[[Category: Cavada, B S]]
[[Category: Cavada BS]]
[[Category: Sol, F Gallego del]]
[[Category: Gallego del Sol F]]
[[Category: Beta-prism]]
[[Category: Lectin]]
[[Category: Sugar binding protein]]
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