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<StructureSection load='6qu9' size='340' side='right'caption='[[6qu9]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6qu9' size='340' side='right'caption='[[6qu9]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6qu9]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6qu9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QU9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6qu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qu9 OCA], [https://pdbe.org/6qu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qu9 RCSB], [https://www.ebi.ac.uk/pdbsum/6qu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qu9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self-association of proteins into ordered aggregates. alpha1-Antitrypsin deficiency is the archetypal serpinopathy and results from the formation and deposition of mutant forms of alpha1-antitrypsin as "polymer" chains in liver tissue. No detailed structural analysis has been performed of this material. Moreover, there is little information on the relevance of well-studied artificially induced polymers to these disease-associated molecules. We have isolated polymers from the liver tissue of Z alpha1-antitrypsin homozygotes (E342K) who have undergone transplantation, labeled them using a Fab fragment, and performed single-particle analysis of negative-stain electron micrographs. The data show structural equivalence between heat-induced and ex vivo polymers and that the intersubunit linkage is best explained by a carboxyl-terminal domain swap between molecules of alpha1-antitrypsin. | |||
The structural basis for Z alpha1-antitrypsin polymerization in the liver.,Faull SV, Elliston ELK, Gooptu B, Jagger AM, Aldobiyan I, Redzej A, Badaoui M, Heyer-Chauhan N, Rashid ST, Reynolds GM, Adams DH, Miranda E, Orlova EV, Irving JA, Lomas DA Sci Adv. 2020 Oct 21;6(43). pii: 6/43/eabc1370. doi: 10.1126/sciadv.abc1370., Print 2020 Oct. PMID:33087346<ref>PMID:33087346</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6qu9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Heyer-Chauhan | [[Category: Heyer-Chauhan N]] | ||
[[Category: Irving | [[Category: Irving JA]] | ||
[[Category: Jagger | [[Category: Jagger AM]] | ||
[[Category: Lomas | [[Category: Lomas DA]] | ||
Latest revision as of 08:41, 21 November 2024
Fab fragment of an antibody that inhibits polymerisation of alpha-1-antitrypsinFab fragment of an antibody that inhibits polymerisation of alpha-1-antitrypsin
Structural highlights
Publication Abstract from PubMedThe serpinopathies are among a diverse set of conformational diseases that involve the aberrant self-association of proteins into ordered aggregates. alpha1-Antitrypsin deficiency is the archetypal serpinopathy and results from the formation and deposition of mutant forms of alpha1-antitrypsin as "polymer" chains in liver tissue. No detailed structural analysis has been performed of this material. Moreover, there is little information on the relevance of well-studied artificially induced polymers to these disease-associated molecules. We have isolated polymers from the liver tissue of Z alpha1-antitrypsin homozygotes (E342K) who have undergone transplantation, labeled them using a Fab fragment, and performed single-particle analysis of negative-stain electron micrographs. The data show structural equivalence between heat-induced and ex vivo polymers and that the intersubunit linkage is best explained by a carboxyl-terminal domain swap between molecules of alpha1-antitrypsin. The structural basis for Z alpha1-antitrypsin polymerization in the liver.,Faull SV, Elliston ELK, Gooptu B, Jagger AM, Aldobiyan I, Redzej A, Badaoui M, Heyer-Chauhan N, Rashid ST, Reynolds GM, Adams DH, Miranda E, Orlova EV, Irving JA, Lomas DA Sci Adv. 2020 Oct 21;6(43). pii: 6/43/eabc1370. doi: 10.1126/sciadv.abc1370., Print 2020 Oct. PMID:33087346[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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