2mll: Difference between revisions
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==MISTLETOE LECTIN I FROM VISCUM ALBUM== | ==MISTLETOE LECTIN I FROM VISCUM ALBUM== | ||
<StructureSection load='2mll' size='340' side='right' caption='[[2mll]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2mll' size='340' side='right'caption='[[2mll]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mll]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2mll]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Viscum_album Viscum album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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]] 2.7Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2mll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mll OCA], [https://pdbe.org/2mll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mll RCSB], [https://www.ebi.ac.uk/pdbsum/2mll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mll ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ML4_VISAL ML4_VISAL] The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.<ref>PMID:15001393</ref> <ref>PMID:1450445</ref> [UniProtKB:P81446] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ml/2mll_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ml/2mll_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2mll" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2mll" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Viscum album]] | [[Category: Viscum album]] | ||
[[Category: Betzel | [[Category: Betzel C]] | ||
[[Category: Eschenburg | [[Category: Eschenburg S]] | ||
[[Category: Konareva | [[Category: Konareva N]] | ||
[[Category: Kornilov | [[Category: Kornilov V]] | ||
[[Category: Krauspenhaar | [[Category: Krauspenhaar R]] | ||
[[Category: Maier | [[Category: Maier T]] | ||
[[Category: Mikailova | [[Category: Mikailova I]] | ||
[[Category: Mikhailov | [[Category: Mikhailov A]] | ||
[[Category: Perbandt | [[Category: Perbandt M]] | ||
[[Category: Singh | [[Category: Singh TP]] | ||
[[Category: Stoeva | [[Category: Stoeva S]] | ||
[[Category: Voelter | [[Category: Voelter W]] | ||
[[Category: Wacker | [[Category: Wacker R]] | ||
Latest revision as of 04:12, 21 November 2024
MISTLETOE LECTIN I FROM VISCUM ALBUMMISTLETOE LECTIN I FROM VISCUM ALBUM
Structural highlights
FunctionML4_VISAL The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.[1] [2] [UniProtKB:P81446] 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 structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album has been solved by molecular replacement techniques. The structure has been refined to a crystallographic R-factor of 24.5% using X-ray diffraction data to 2.8 A resolution. The heterodimeric 63-kDa protein consists of a toxic A subunit which exhibits RNA-glycosidase activity and a galactose-specific lectin B subunit. The overall protein fold is similar to that of ricin from Ricinus communis; however, unlike ricin, ML-I is already medically applied as a component of a commercially available misteltoe extract with immunostimulating potency and for the treatment of human cancer. The three-dimensional structure reported here revealed structural details of this pharmaceutically important protein. The comparison to the structure of ricin gives more insights into the functional mechanism of this protein, provides structural details for further protein engineering studies, and may lead to the development of more effective therapeutic RIPs. Crystal structure of mistletoe lectin I from Viscum album.,Krauspenhaar R, Eschenburg S, Perbandt M, Kornilov V, Konareva N, Mikailova I, Stoeva S, Wacker R, Maier T, Singh T, Mikhailov A, Voelter W, Betzel C Biochem Biophys Res Commun. 1999 Apr 13;257(2):418-24. PMID:10198229[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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