2x44: Difference between revisions
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==STRUCTURE OF A STRAND-SWAPPED DIMERIC FORM OF CTLA-4== | |||
<StructureSection load='2x44' size='340' side='right' caption='[[2x44]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x44]] is a 1 chain structure with 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=2X44 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X44 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ah1|1ah1]], [[1h6e|1h6e]], [[1i8l|1i8l]], [[1i85|1i85]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x44 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x44 RCSB], [http://www.ebi.ac.uk/pdbsum/2x44 PDBsum]</span></td></tr> | |||
</table> | |||
== 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/x4/2x44_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis-trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand swapping. Our results suggest a molecular basis for the pathological aggregation of immunoglobulin domains and why amyloid-like fibres are more often composed of homologous rather than heterologous subunits. | |||
Domain metastability: a molecular basis for immunoglobulin deposition?,Sonnen AF, Yu C, Evans EJ, Stuart DI, Davis SJ, Gilbert RJ J Mol Biol. 2010 Jun 4;399(2):207-13. Epub 2010 Apr 13. PMID:20394753<ref>PMID:20394753</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Davis, S J | [[Category: Davis, S J]] | ||
[[Category: Evans, E J | [[Category: Evans, E J]] | ||
[[Category: Gilbert, R J.C | [[Category: Gilbert, R J.C]] | ||
[[Category: Sonnen, A F.P | [[Category: Sonnen, A F.P]] | ||
[[Category: Stuart, D I | [[Category: Stuart, D I]] | ||
[[Category: Yu, C | [[Category: Yu, C]] | ||
[[Category: Amyloidogenic]] | [[Category: Amyloidogenic]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] |
Revision as of 14:15, 18 December 2014
STRUCTURE OF A STRAND-SWAPPED DIMERIC FORM OF CTLA-4STRUCTURE OF A STRAND-SWAPPED DIMERIC FORM OF CTLA-4
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis-trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand swapping. Our results suggest a molecular basis for the pathological aggregation of immunoglobulin domains and why amyloid-like fibres are more often composed of homologous rather than heterologous subunits. Domain metastability: a molecular basis for immunoglobulin deposition?,Sonnen AF, Yu C, Evans EJ, Stuart DI, Davis SJ, Gilbert RJ J Mol Biol. 2010 Jun 4;399(2):207-13. Epub 2010 Apr 13. PMID:20394753[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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