1zgr
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== 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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 19: | ||
</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®/PubMed®, 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/> | ||
| Line 34: | Line 25: | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Parkia platycephala]] | [[Category: Parkia platycephala]] | ||
| - | [[Category: Calvete | + | [[Category: Calvete JJ]] |
| - | [[Category: Cavada | + | [[Category: Cavada BS]] |
| - | [[Category: Sol | + | [[Category: Gallego del Sol F]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the Parkia platycephala seed lectin
| |||||||||||
