1erg: Difference between revisions
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New page: left|200px<br /> <applet load="1erg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1erg" /> '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE... |
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== | ==THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE EXTRACELLULAR REGION OF THE COMPLEMENT REGULATORY PROTEIN, CD59, A NEW CELL SURFACE PROTEIN DOMAIN RELATED TO NEUROTOXINS== | ||
The cell surface antigen CD59 is an inhibitor of complement-mediated lysis | <StructureSection load='1erg' size='340' side='right'caption='[[1erg]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1erg]] 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=1ERG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ERG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1erg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erg OCA], [https://pdbe.org/1erg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1erg RCSB], [https://www.ebi.ac.uk/pdbsum/1erg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1erg ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[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> | |||
== Function == | |||
[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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/1erg_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1erg ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cell surface antigen CD59 is an inhibitor of complement-mediated lysis and a member of the Ly6 superfamily (Ly6SF) of cysteine-rich cell-surface molecules whose sequences are related to those of snake venom neurotoxins. The three-dimensional solution structure of a recombinant form of the extracellular region of the molecule (residues 1-70 of the mature protein; sCD59) has been solved by 2D NMR methods. sCD59 is a relatively flat, disk-shaped molecule consisting of a two-standed beta-sheet finger loosely packed against a protein core formed by a three-stranded beta-sheet and a short helix. Structure calculations allowed an unambiguous assignment of the disulfide-bonded cysteine pairs as 3-26, 6-13, 19-39, 45-63, and 64-69. The topology of sCD59 is similar to that of the snake venom neurotoxins and consistent with an evolutionary relationship existing between the Ly6SF and the neurotoxins. | |||
Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins.,Kieffer B, Driscoll PC, Campbell ID, Willis AC, van der Merwe PA, Davis SJ Biochemistry. 1994 Apr 19;33(15):4471-82. PMID:7512825<ref>PMID:7512825</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1erg" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[CD59|CD59]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Campbell | [[Category: Campbell ID]] | ||
[[Category: Davis | [[Category: Davis SJ]] | ||
[[Category: Driscoll | [[Category: Driscoll PC]] | ||
[[Category: Kieffer | [[Category: Kieffer B]] | ||
[[Category: | [[Category: Van Der Merwe PA]] | ||
[[Category: Willis | [[Category: Willis AC]] | ||
Latest revision as of 04:29, 17 October 2024
THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE EXTRACELLULAR REGION OF THE COMPLEMENT REGULATORY PROTEIN, CD59, A NEW CELL SURFACE PROTEIN DOMAIN RELATED TO NEUROTOXINS
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