1hup
From Proteopedia
(Difference between revisions)
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<StructureSection load='1hup' size='340' side='right'caption='[[1hup]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1hup' size='340' side='right'caption='[[1hup]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1hup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1hup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HUP FirstGlance]. <br> |
| - | </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=SO4:SULFATE+ION'>SO4</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]] 2.5Å</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=SO4:SULFATE+ION'>SO4</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=1hup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hup OCA], [https://pdbe.org/1hup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hup RCSB], [https://www.ebi.ac.uk/pdbsum/1hup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hup ProSAT]</span></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=1hup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hup OCA], [https://pdbe.org/1hup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hup RCSB], [https://www.ebi.ac.uk/pdbsum/1hup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hup ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/MBL2_HUMAN MBL2_HUMAN] 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. May bind DNA.<ref>PMID:14515269</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1hup ConSurf]. | </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=1hup ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Human mannose-binding protein is a hexamer of trimers with each subunit consisting of an amino-terminal region rich in cysteine, 19 collagen repeats, a 'neck', and a carbohydrate recognition domain that requires calcium to bind ligand. A 148-residue peptide, consisting of the 'neck' and carbohydrate recognition domains forms trimers in solution and in crystals. The structure of this trimeric peptide has been determined in two different crystal forms. The 'neck' forms a triple alpha-helical coiled-coil. Each alpha-helix interacts with a neighbouring carbohydrate recognition domain. The spatial arrangement of the carbohydrate recognition domains suggest how MBP trimers form the basic recognition unit for branched oligosaccharides on microorganisms. | ||
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| - | Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil.,Sheriff S, Chang CY, Ezekowitz RA Nat Struct Biol. 1994 Nov;1(11):789-94. PMID:7634089<ref>PMID:7634089</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1hup" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Sheriff | + | [[Category: Sheriff S]] |
| - | + | ||
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Revision as of 11:35, 27 March 2024
HUMAN MANNOSE BINDING PROTEIN CARBOHYDRATE RECOGNITION DOMAIN TRIMERIZES THROUGH A TRIPLE ALPHA-HELICAL COILED-COIL
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