1ciw: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ciw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CIW FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ciw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CIW FirstGlance]. <br> | ||
</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= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PRD_900019:N-acetyl-alpha-lactosamine'>PRD_900019</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=1ciw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ciw OCA], [https://pdbe.org/1ciw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ciw RCSB], [https://www.ebi.ac.uk/pdbsum/1ciw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ciw 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=1ciw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ciw OCA], [https://pdbe.org/1ciw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ciw RCSB], [https://www.ebi.ac.uk/pdbsum/1ciw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ciw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/LECG_ARAHY LECG_ARAHY] D-galactose specific lectin. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Arachis hypogaea]] | [[Category: Arachis hypogaea]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ravishankar | [[Category: Ravishankar R]] | ||
[[Category: Suguna | [[Category: Suguna K]] | ||
[[Category: Surolia | [[Category: Surolia A]] | ||
[[Category: Vijayan | [[Category: Vijayan M]] | ||
Revision as of 02:26, 28 December 2023
PEANUT LECTIN COMPLEXED WITH N-ACETYLLACTOSAMINEPEANUT LECTIN COMPLEXED WITH N-ACETYLLACTOSAMINE
Structural highlights
FunctionLECG_ARAHY D-galactose specific lectin. Evolutionary 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 structures of complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine have been determined at 2.8 and 2.7 A, respectively. These, and the complexes involving lactose and the T-antigenic disaccharide reported previously, permit a detailed characterization of peanut-lectin-carbohydrate association and the role of water molecules therein. The water molecules in the combining site are substantially conserved in the four complexes. The role of interacting sugar hydroxyl groups, when absent, are often mimicked by ordered water molecules not only at the primary combining site, but also at the site of the second sugar ring. The similarity of peanut-lectin-sugar interactions with those in other galactose/N-acetylgalactosamine-specific lectins also extend to a substantial degree to water bridges. The comparative study provides a structural explanation for the exclusive specificity of peanut lectin for galactose at the monosaccharide level, compared with that of the other lectins for galactose as well as N-acetylgalactosamine. The complexes also provide a qualitative structural rationale for differences in the strengths of binding of peanut lectin to different sugars. Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins.,Ravishankar R, Suguna K, Surolia A, Vijayan M Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1375-82. PMID:10417405[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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