1kwx

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[[Image:1kwx.gif|left|200px]]
 
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{{Structure
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==Rat mannose protein A complexed with b-Me-Fuc.==
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|PDB= 1kwx |SIZE=350|CAPTION= <scene name='initialview01'>1kwx</scene>, resolution 2.00&Aring;
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<StructureSection load='1kwx' size='340' side='right'caption='[[1kwx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MFB:BETA-L-METHYL-FUCOSE'>MFB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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<table><tr><td colspan='2'>[[1kwx]] 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=1KWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KWX FirstGlance]. <br>
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|ACTIVITY=
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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]] 2&#8491;</td></tr>
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|GENE= MBL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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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=MFB:BETA-L-METHYL-FUCOSE'>MFB</scene></td></tr>
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}}
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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=1kwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwx OCA], [https://pdbe.org/1kwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kwx RCSB], [https://www.ebi.ac.uk/pdbsum/1kwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwx 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/kw/1kwx_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=1kwx ConSurf].
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<div style="clear:both"></div>
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'''Rat mannose protein A complexed with b-Me-Fuc.'''
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==See Also==
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*[[Mannose-binding protein|Mannose-binding protein]]
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__TOC__
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==Overview==
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</StructureSection>
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Mannose-binding proteins (MBPs) are C-type animal lectins that recognize high mannose oligosaccharides on pathogenic cell surfaces. MBPs bind to their carbohydrate ligands by forming a series of Ca(2+) coordination and hydrogen bonds with two hydroxyl groups equivalent to the 3- and 4-OH of mannose. In this work, the determinants of the orientation of sugars bound to rat serum and liver MBPs (MBP-A and MBP-C) have been systematically investigated. The crystal structures of MBP-A soaked with monosaccharides and disaccharides and also the structure of the MBP-A trimer cross-linked by a high mannose asparaginyl oligosaccharide reveal that monosaccharides or alpha1-6-linked mannose bind to MBP-A in one orientation, whereas alpha1-2- or alpha1-3-linked mannose binds in an orientation rotated 180 degrees around a local symmetry axis relating the 3- and 4-OH groups. In contrast, a similar set of ligands all bind to MBP-C in a single orientation. The mutation of MBP-A His(189) to its MBP-C equivalent, valine, causes Man alpha 1-3Man to bind in a mixture of orientations. These data combined with modeling indicate that the residue at this position influences the orientation of bound ligands in MBP. We propose that the control of binding orientation can influence the recognition of multivalent ligands. A lateral association of trimers in the cross-linked crystals may reflect interactions within higher oligomers of MBP-A that are stabilized by multivalent ligands.
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[[Category: Large Structures]]
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==About this Structure==
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1KWX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWX OCA].
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==Reference==
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Orientation of bound ligands in mannose-binding proteins. Implications for multivalent ligand recognition., Ng KK, Kolatkar AR, Park-Snyder S, Feinberg H, Clark DA, Drickamer K, Weis WI, J Biol Chem. 2002 May 3;277(18):16088-95. Epub 2002 Feb 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11850428 11850428]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Clark DA]]
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[[Category: Clark, D A.]]
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[[Category: Drickamer K]]
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[[Category: Drickamer, K.]]
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[[Category: Feinberg H]]
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[[Category: Feinberg, H.]]
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[[Category: Kolatkar AR]]
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[[Category: Kolatkar, A R.]]
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[[Category: Ng KK]]
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[[Category: Ng, K K.]]
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[[Category: Park-Snyder S]]
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[[Category: Park-Snyder, S.]]
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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: MFB]]
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[[Category: c-type lectin]]
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[[Category: calcium-binding protein]]
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[[Category: lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:23:16 2008''
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Current revision

Rat mannose protein A complexed with b-Me-Fuc.

PDB ID 1kwx

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