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1cds

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(New page: 200px<br /> <applet load="1cds" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cds" /> '''STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM O...)
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[[Image:1cds.gif|left|200px]]<br />
 
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<applet load="1cds" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cds" />
 
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'''STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT REGULATORY PROTEIN CD59'''<br />
 
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==Overview==
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==STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT REGULATORY PROTEIN CD59==
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BACKGROUND: CD59 is a cell-surface glycoprotein that protects host cells, from complement-mediated lysis by binding to and preventing the normal, functioning of the complement proteins C8 and/or C9 which form part of a, membrane penetrating assembly called the membrane attack complex. CD59 has, no structural similarity to other complement proteins, but is an example, of a plasma protein domain type found also in murine Ly-6 proteins and the, urokinase-type plasminogen activator receptor. RESULTS: CD59 was purified, from human urine, retaining the N-glycan and at least some of the, non-lipid component of the glycosylphosphatidylinositol membrane anchor., The three-dimensional structure of the protein component has been, determined in the presence of the carbohydrate groups using, two-dimensional NMR spectroscopy. The protein structure is well defined by, the NMR data (root mean square deviation from the mean structure of 0.65 A, for backbone atoms and no distance constraint violations greater than 0.4, A). Structure calculations were also carried out to model the orientation, of the N-acetylglucosamine residue that is directly linked to Asn18., CONCLUSIONS: The main features of the protein structure are two, antiparallel beta-sheets (a central one with three strands and another, with two), a short helix that packs against the three-stranded beta-sheet, and a carboxy-terminal region that, although lacking regular secondary, structure, is well defined and packs against the three-stranded, beta-sheet, on the opposite face to the helix. We have used the structure, in combination with existing biochemical data, to identify residues that, may be involved in C8 binding.
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<StructureSection load='1cds' size='340' side='right'caption='[[1cds]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cds]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CDS 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">Solution NMR</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=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=1cds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cds OCA], [https://pdbe.org/1cds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cds RCSB], [https://www.ebi.ac.uk/pdbsum/1cds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cds ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CD59_HUMAN CD59_HUMAN] Defects in CD59 are the cause of CD59 deficiency (CD59D) [MIM:[https://omim.org/entry/612300 612300].<ref>PMID:1382994</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/CD59_HUMAN CD59_HUMAN] Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase. The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.
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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/cd/1cds_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=1cds ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: CD59 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107271 107271]]
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*[[CD59|CD59]]
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== References ==
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==About this Structure==
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<references/>
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1CDS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CDS OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Homo sapiens]]
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Structure of a soluble, glycosylated form of the human complement regulatory protein CD59., Fletcher CM, Harrison RA, Lachmann PJ, Neuhaus D, Structure. 1994 Mar 15;2(3):185-99. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7520819 7520819]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Fletcher CM]]
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[[Category: Fletcher, C.M.]]
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[[Category: Harrison RA]]
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[[Category: Harrison, R.A.]]
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[[Category: Lachmann PJ]]
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[[Category: Lachmann, P.J.]]
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[[Category: Neuhaus D]]
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[[Category: Neuhaus, D.]]
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[[Category: complement regulatory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:20:41 2007''
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Current revision

STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT REGULATORY PROTEIN CD59

PDB ID 1cds

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