2x89: Difference between revisions
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==Structure of the Beta2_microglobulin involved in amyloidogenesis== | |||
<StructureSection load='2x89' size='340' side='right'caption='[[2x89]], [[Resolution|resolution]] 2.16Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x89]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X89 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16Å</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=2x89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x89 OCA], [https://pdbe.org/2x89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x89 RCSB], [https://www.ebi.ac.uk/pdbsum/2x89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x89 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A2KD59_LAMGL A2KD59_LAMGL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Atomic-level structural investigation of the key conformational intermediates of amyloidogenesis remains a challenge. Here we demonstrate the utility of nanobodies to trap and characterize intermediates of beta2-microglobulin (beta2m) amyloidogenesis by X-ray crystallography. For this purpose, we selected five single domain antibodies that block the fibrillogenesis of a proteolytic amyloidogenic fragment of beta2m (DeltaN6beta2m). The crystal structure of DeltaN6beta2m in complex with one of these nanobodies (Nb24) identifies domain swapping as a plausible mechanism of self-association of this amyloidogenic protein. In the swapped dimer, two extended hinge loops-corresponding to the heptapetide NHVTLSQ that forms amyloid in isolation-are unmasked and fold into a new two-stranded antiparallel beta-sheet. The beta-strands of this sheet are prone to self-associate and stack perpendicular to the direction of the strands to build large intermolecular beta-sheets that run parallel to the axis of growing oligomers, providing an elongation mechanism by self-templated growth. | |||
Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic {beta}2-microglobulin variant.,Domanska K, Vanderhaegen S, Srinivasan V, Pardon E, Dupeux F, Marquez JA, Giorgetti S, Stoppini M, Wyns L, Bellotti V, Steyaert J Proc Natl Acad Sci U S A. 2011 Jan 10. PMID:21220305<ref>PMID:21220305</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x89" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Beta-2 microglobulin|Beta-2 microglobulin]] | *[[Antibody 3D structures|Antibody 3D structures]] | ||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
== | *[[3D structures of non-human antibody|3D structures of non-human antibody]] | ||
< | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Camelus dromedarius]] | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bellotti | [[Category: Large Structures]] | ||
[[Category: Domanska | [[Category: Bellotti V]] | ||
[[Category: Marquez | [[Category: Domanska K]] | ||
[[Category: Pardon | [[Category: Marquez JA]] | ||
[[Category: Srinivasan | [[Category: Pardon E]] | ||
[[Category: Steyaert | [[Category: Srinivasan V]] | ||
[[Category: Vanderhaegen | [[Category: Steyaert J]] | ||
[[Category: Wyns | [[Category: Vanderhaegen S]] | ||
[[Category: Wyns L]] | |||
Latest revision as of 13:26, 20 December 2023
Structure of the Beta2_microglobulin involved in amyloidogenesisStructure of the Beta2_microglobulin involved in amyloidogenesis
Structural highlights
FunctionPublication Abstract from PubMedAtomic-level structural investigation of the key conformational intermediates of amyloidogenesis remains a challenge. Here we demonstrate the utility of nanobodies to trap and characterize intermediates of beta2-microglobulin (beta2m) amyloidogenesis by X-ray crystallography. For this purpose, we selected five single domain antibodies that block the fibrillogenesis of a proteolytic amyloidogenic fragment of beta2m (DeltaN6beta2m). The crystal structure of DeltaN6beta2m in complex with one of these nanobodies (Nb24) identifies domain swapping as a plausible mechanism of self-association of this amyloidogenic protein. In the swapped dimer, two extended hinge loops-corresponding to the heptapetide NHVTLSQ that forms amyloid in isolation-are unmasked and fold into a new two-stranded antiparallel beta-sheet. The beta-strands of this sheet are prone to self-associate and stack perpendicular to the direction of the strands to build large intermolecular beta-sheets that run parallel to the axis of growing oligomers, providing an elongation mechanism by self-templated growth. Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic {beta}2-microglobulin variant.,Domanska K, Vanderhaegen S, Srinivasan V, Pardon E, Dupeux F, Marquez JA, Giorgetti S, Stoppini M, Wyns L, Bellotti V, Steyaert J Proc Natl Acad Sci U S A. 2011 Jan 10. PMID:21220305[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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