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| | <StructureSection load='3dvi' size='340' side='right'caption='[[3dvi]], [[Resolution|resolution]] 1.53Å' scene=''> | | <StructureSection load='3dvi' size='340' side='right'caption='[[3dvi]], [[Resolution|resolution]] 1.53Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dvi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DVI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dvi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DVI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2q20|2q20]], [[2q1e|2q1e]]</div></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]] 1.53Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mutant of vk1 o18/o8 germline ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3dvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dvi OCA], [https://pdbe.org/3dvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dvi RCSB], [https://www.ebi.ac.uk/pdbsum/3dvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dvi ProSAT]</span></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=3dvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dvi OCA], [https://pdbe.org/3dvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dvi RCSB], [https://www.ebi.ac.uk/pdbsum/3dvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dvi ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ramirez-Alvarado, M]] | + | [[Category: Ramirez-Alvarado M]] |
| - | [[Category: Randles, E G]] | + | [[Category: Randles EG]] |
| - | [[Category: Thompson, J R]] | + | [[Category: Thompson JR]] |
| - | [[Category: Al]]
| + | |
| - | [[Category: Amyloid]]
| + | |
| - | [[Category: Immunoglobulin]]
| + | |
| - | [[Category: Light chain]]
| + | |
| - | [[Category: Light chain amyloidosis]]
| + | |
| - | [[Category: Light chain variable domain]]
| + | |
| - | [[Category: Protein fibril]]
| + | |
| 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 PubMed
Amyloid diseases are characterized by the misfolding of a precursor protein that leads to amyloid fibril formation. Despite the fact that there are different precursors, some commonalities in the misfolding mechanism are thought to exist. In light chain amyloidosis (AL), the immunoglobulin light chain forms amyloid fibrils that deposit in the extracellular space of vital organs. AL proteins are thermodynamically destabilized compared to non-amyloidogenic proteins and some studies have linked this instability to increased fibril formation rates. Here we present the crystal structures of two highly homologous AL proteins, AL-12 and AL-103. This structural study shows that these proteins retain the canonical germ line dimer interface. We highlight important structural alterations in two loops flanking the dimer interface and correlate these results with the somatic mutations present in AL-12 and AL-103. We suggest that these alterations are informative structural features that are likely contributing to protein instability that leads to conformational changes involved in the initial events of amyloid formation.
Structural alterations within native amyloidogenic immunoglobulin light chains.,Randles EG, Thompson JR, Martin DJ, Ramirez-Alvarado M J Mol Biol. 2009 May 29;389(1):199-210. Epub 2009 Apr 8. PMID:19361523[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Randles EG, Thompson JR, Martin DJ, Ramirez-Alvarado M. Structural alterations within native amyloidogenic immunoglobulin light chains. J Mol Biol. 2009 May 29;389(1):199-210. Epub 2009 Apr 8. PMID:19361523 doi:10.1016/j.jmb.2009.04.010
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