2jhk

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[[Image:2jhk.jpg|left|200px]]
 
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{{Structure
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==Structure of globular heads of M-ficolin complexed with N-acetyl-D- glucosamine==
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|PDB= 2jhk |SIZE=350|CAPTION= <scene name='initialview01'>2jhk</scene>, resolution 1.75&Aring;
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<StructureSection load='2jhk' size='340' side='right'caption='[[2jhk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+F'>AC1</scene> and <scene name='pdbsite=AC2:Nag+Binding+Site+For+Chain+F'>AC2</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[2jhk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JHK FirstGlance]. <br>
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|ACTIVITY=
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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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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|GENE=
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jhh|2jhh]], [[2jhi|2jhi]], [[2jhl|2jhl]], [[2jhm|2jhm]]</div></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=2jhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jhk OCA], [https://pdbe.org/2jhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jhk RCSB], [https://www.ebi.ac.uk/pdbsum/2jhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jhk ProSAT]</span></td></tr>
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</table>
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'''STRUCTURE OF GLOBULAR HEADS OF M-FICOLIN COMPLEXED WITH N-ACETYL-D-GLUCOSAMINE'''
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== Function ==
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[[https://www.uniprot.org/uniprot/FCN1_HUMAN FCN1_HUMAN]] Complement-activating lectin and pattern recognition receptor. Binds GlcNAc. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage.<ref>PMID:20032467</ref>
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== Evolutionary Conservation ==
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==Overview==
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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/jh/2jhk_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=2jhk 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 ==
Ficolins are soluble oligomeric proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains. They act as innate immune sensors by recognizing conserved molecular markers exposed on microbial surfaces and thereby triggering effector mechanisms such as enhanced phagocytosis and inflammation. In humans, L- and H-ficolins have been characterized in plasma, whereas a third species, M-ficolin, is secreted by monocytes and macrophages. To decipher the molecular mechanisms underlying their recognition properties, we previously solved the structures of the recognition domains of L- and H-ficolins, in complex with various model ligands (Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J. C., Arlaud, G. J., Thielens, N. M., and Gaboriaud, C. (2007) EMBO J. 24, 623-633). We now report the ligand-bound crystal structures of the recognition domain of M-ficolin, determined at high resolution (1.75-1.8 A), which provides the first structural insights into its binding properties. Interaction with acetylated carbohydrates differs from the one previously described for L-ficolin. This study also reveals the structural determinants for binding to sialylated compounds, a property restricted to human M-ficolin and its mouse counterpart, ficolin B. Finally, comparison between the ligand-bound structures obtained at neutral pH and nonbinding conformations observed at pH 5.6 reveals how the ligand binding site is dislocated at acidic pH. This means that the binding function of M-ficolin is subject to a pH-sensitive conformational switch. Considering that the homologous ficolin B is found in the lysosomes of activated macrophages (Runza, V. L., Hehlgans, T., Echtenacher, B., Zahringer, U., Schwaeble, W. J., and Mannel, D. N. (2006) J. Endotoxin Res. 12, 120-126), we propose that this switch could play a physiological role in such acidic compartments.
Ficolins are soluble oligomeric proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains. They act as innate immune sensors by recognizing conserved molecular markers exposed on microbial surfaces and thereby triggering effector mechanisms such as enhanced phagocytosis and inflammation. In humans, L- and H-ficolins have been characterized in plasma, whereas a third species, M-ficolin, is secreted by monocytes and macrophages. To decipher the molecular mechanisms underlying their recognition properties, we previously solved the structures of the recognition domains of L- and H-ficolins, in complex with various model ligands (Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J. C., Arlaud, G. J., Thielens, N. M., and Gaboriaud, C. (2007) EMBO J. 24, 623-633). We now report the ligand-bound crystal structures of the recognition domain of M-ficolin, determined at high resolution (1.75-1.8 A), which provides the first structural insights into its binding properties. Interaction with acetylated carbohydrates differs from the one previously described for L-ficolin. This study also reveals the structural determinants for binding to sialylated compounds, a property restricted to human M-ficolin and its mouse counterpart, ficolin B. Finally, comparison between the ligand-bound structures obtained at neutral pH and nonbinding conformations observed at pH 5.6 reveals how the ligand binding site is dislocated at acidic pH. This means that the binding function of M-ficolin is subject to a pH-sensitive conformational switch. Considering that the homologous ficolin B is found in the lysosomes of activated macrophages (Runza, V. L., Hehlgans, T., Echtenacher, B., Zahringer, U., Schwaeble, W. J., and Mannel, D. N. (2006) J. Endotoxin Res. 12, 120-126), we propose that this switch could play a physiological role in such acidic compartments.
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==About this Structure==
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Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch.,Garlatti V, Martin L, Gout E, Reiser JB, Fujita T, Arlaud GJ, Thielens NM, Gaboriaud C J Biol Chem. 2007 Dec 7;282(49):35814-20. Epub 2007 Sep 26. PMID:17897951<ref>PMID:17897951</ref>
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2JHK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JHK 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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Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch., Garlatti V, Martin L, Gout E, Reiser JB, Fujita T, Arlaud GJ, Thielens NM, Gaboriaud C, J Biol Chem. 2007 Dec 7;282(49):35814-20. Epub 2007 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17897951 17897951]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2jhk" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Arlaud, G J.]]
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[[Category: Gaboriaud, C.]]
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[[Category: Garlatti, V.]]
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[[Category: Gout, E.]]
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[[Category: Martin, L.]]
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[[Category: Reiser, J B.]]
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[[Category: Thielens, N M.]]
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[[Category: CA]]
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[[Category: NAG]]
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[[Category: acidic ph]]
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[[Category: collagen]]
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[[Category: complement]]
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[[Category: glycoprotein]]
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[[Category: innate immunity]]
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[[Category: lectin]]
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[[Category: polymorphism]]
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[[Category: sugar-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:42:01 2008''
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==See Also==
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*[[Ficolin|Ficolin]]
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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: Human]]
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[[Category: Large Structures]]
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[[Category: Arlaud, G J]]
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[[Category: Gaboriaud, C]]
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[[Category: Garlatti, V]]
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[[Category: Gout, E]]
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[[Category: Martin, L]]
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[[Category: Reiser, J B]]
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[[Category: Thielens, N M]]
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[[Category: Acidic ph]]
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[[Category: Collagen]]
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[[Category: Complement]]
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[[Category: Glycoprotein]]
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[[Category: Innate immunity]]
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[[Category: Lectin]]
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[[Category: Polymorphism]]
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[[Category: Sugar binding protein]]
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[[Category: Sugar-binding protein]]

Current revision

Structure of globular heads of M-ficolin complexed with N-acetyl-D- glucosamine

PDB ID 2jhk

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