2msb

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(New page: 200px<br /><applet load="2msb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2msb, resolution 1.7&Aring;" /> '''STRUCTURE OF A C-TYPE...)
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[[Image:2msb.jpg|left|200px]]<br /><applet load="2msb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2msb, resolution 1.7&Aring;" />
 
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'''STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE'''<br />
 
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==Overview==
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==STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE==
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C-type (Ca(2+)-dependent) animal lectins such as mannose-binding proteins, mediate many cell-surface carbohydrate-recognition events. The crystal, structure at 1.7 A resolution of the carbohydrate-recognition domain of, rat mannose-binding protein complexed with an oligomannose, asparaginyl-oligosaccharide reveals that Ca2+ forms coordination bonds, with the carbohydrate ligand. Carbohydrate specificity is determined by a, network of coordination and hydrogen bonds that stabilizes the ternary, complex of protein, Ca2+ and sugar. Two branches of the oligosaccharide, crosslink neighbouring carbohydrate-recognition domains in the crystal, enabling multivalent binding to a single oligosaccharide chain to be, visualized directly.
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<StructureSection load='2msb' size='340' side='right'caption='[[2msb]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2msb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Black_rat Black rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2msb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msb OCA], [https://pdbe.org/2msb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msb RCSB], [https://www.ebi.ac.uk/pdbsum/2msb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/MBL1_RAT MBL1_RAT]] Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ms/2msb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2msb ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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C-type (Ca(2+)-dependent) animal lectins such as mannose-binding proteins mediate many cell-surface carbohydrate-recognition events. The crystal structure at 1.7 A resolution of the carbohydrate-recognition domain of rat mannose-binding protein complexed with an oligomannose asparaginyl-oligosaccharide reveals that Ca2+ forms coordination bonds with the carbohydrate ligand. Carbohydrate specificity is determined by a network of coordination and hydrogen bonds that stabilizes the ternary complex of protein, Ca2+ and sugar. Two branches of the oligosaccharide crosslink neighbouring carbohydrate-recognition domains in the crystal, enabling multivalent binding to a single oligosaccharide chain to be visualized directly.
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==About this Structure==
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Structure of a C-type mannose-binding protein complexed with an oligosaccharide.,Weis WI, Drickamer K, Hendrickson WA Nature. 1992 Nov 12;360(6400):127-34. PMID:1436090<ref>PMID:1436090</ref>
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2MSB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2MSB OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of a C-type mannose-binding protein complexed with an oligosaccharide., Weis WI, Drickamer K, Hendrickson WA, Nature. 1992 Nov 12;360(6400):127-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1436090 1436090]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 2msb" style="background-color:#fffaf0;"></div>
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[[Category: Drickamer, K.]]
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[[Category: Hendrickson, W.A.]]
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[[Category: Weis, W.I.]]
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[[Category: CA]]
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[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:45:52 2007''
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==See Also==
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*[[Mannose-binding protein|Mannose-binding protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Black rat]]
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[[Category: Large Structures]]
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[[Category: Drickamer, K]]
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[[Category: Hendrickson, W A]]
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[[Category: Weis, W I]]
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[[Category: Lectin]]

Current revision

STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE

PDB ID 2msb

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