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1rtm

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(New page: 200px<br /><applet load="1rtm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rtm, resolution 1.8&Aring;" /> '''TRIMERIC STRUCTURE OF...)
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[[Image:1rtm.gif|left|200px]]<br /><applet load="1rtm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rtm, resolution 1.8&Aring;" />
 
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'''TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN'''<br />
 
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==Overview==
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==TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN==
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BACKGROUND: Mannose-binding proteins (MBPs) are C-type (Ca(2+)-dependent), animal lectins found in serum. They recognize cell-surface oligosaccharide, structures characteristic of pathogenic bacteria and fungi, and trigger, the neutralization of these organisms. Like most lectins, MBPs display, weak intrinsic affinity for monovalent sugar ligands, but bind avidly to, multivalent ligands. RESULTS: We report physical studies in solution and, the crystal structure determined at 1.8 A Bragg spacings of a trimeric, fragment of MBP-A, containing the carbohydrate-recognition domain (CRD), and the neck domain that links the carboxy-terminal CRD to the, collagen-like portion of the intact molecule. The neck consists of a, parallel triple-stranded coiled coil of alpha-helices linked by four, residues to the CRD. The isolated neck peptide does not form stable, helices in aqueous solution. The previously characterized, carbohydrate-binding sites lie at the distal end of the trimer and are, separated from each other by 53 A. CONCLUSIONS: The carbohydrate-binding, sites in MBP-A are too far apart for a single trimer to bind multivalently, to a typical mammalian high-mannose oligosaccharide. Thus MBPs can, recognize pathogens selectively by binding avidly only to the widely, spaced, repetitive sugar arrays on pathogenic cell surfaces. Sequence, alignments reveal that other C-type lectins are likely to have a similar, oligomeric structure, but differences in their detailed organization will, have an important role in determining their interactions with, oligosaccharides.
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<StructureSection load='1rtm' size='340' side='right'caption='[[1rtm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rtm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RTM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1rtm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rtm OCA], [https://pdbe.org/1rtm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rtm RCSB], [https://www.ebi.ac.uk/pdbsum/1rtm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rtm 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/rt/1rtm_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=1rtm ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1RTM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA, CL and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RTM OCA].
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*[[Mannose-binding protein|Mannose-binding protein]]
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__TOC__
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==Reference==
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</StructureSection>
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Trimeric structure of a C-type mannose-binding protein., Weis WI, Drickamer K, Structure. 1994 Dec 15;2(12):1227-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7704532 7704532]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Drickamer K]]
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[[Category: Drickamer, K.]]
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[[Category: Weis WI]]
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[[Category: Weis, W.I.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: GOL]]
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[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:51:36 2007''
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Current revision

TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN

PDB ID 1rtm

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