2q1e

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[[Image:2q1e.jpg|left|200px]]
 
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==Altered dimer interface decreases stability in an amyloidogenic kappa1 Bence Jones protein.==
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The line below this paragraph, containing "STRUCTURE_2q1e", creates the "Structure Box" on the page.
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<StructureSection load='2q1e' size='340' side='right'caption='[[2q1e]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2q1e]] is a 4 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=2Q1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q1E FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2q1e| PDB=2q1e | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q1e OCA], [https://pdbe.org/2q1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q1e RCSB], [https://www.ebi.ac.uk/pdbsum/2q1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q1e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A2NI60_HUMAN A2NI60_HUMAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Amyloidoses are devastating and currently incurable diseases in which the process of amyloid formation causes fatal cellular and organ damage. The molecular mechanisms underlying amyloidoses are not well known. In this study, we address the structural basis of immunoglobulin light chain amyloidosis, which results from deposition of light chains produced by clonal plasma cells. We compare light chain amyloidosis protein AL-09 to its wild-type counterpart, the kappaI O18/O8 light chain germline. Crystallographic studies indicate that both proteins form dimers. However, AL-09 has an altered dimer interface that is rotated 90 degrees from the kappaI O18/O8 dimer interface. The three non-conservative mutations in AL-09 are located within the dimer interface, consistent with their role in the decreased stability of this amyloidogenic protein. Moreover, AL-09 forms amyloid fibrils more quickly than kappaI O18/O8 in vitro. These results support the notion that the increased stability of the monomer and delayed fibril formation, together with a properly formed dimer, may be protective against amyloidogenesis. This could open a new direction into rational drug design for amyloidogenic proteins.
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'''Altered dimer interface decreases stability in an amyloidogenic kappa1 Bence Jones protein.'''
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Altered dimer interface decreases stability in an amyloidogenic protein.,Baden EM, Owen BA, Peterson FC, Volkman BF, Ramirez-Alvarado M, Thompson JR J Biol Chem. 2008 Jun 6;283(23):15853-60. Epub 2008 Apr 8. PMID:18400753<ref>PMID:18400753</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==Overview==
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</div>
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Amyloidoses are devastating and currently incurable diseases in which the process of amyloid formation causes fatal cellular and organ damage. The molecular mechanisms underlying amyloidoses are not well known. In this study, we address the structural basis of immunoglobulin light chain amyloidosis, which results from deposition of light chains produced by clonal plasma cells. We compare light chain amyloidosis protein AL-09 to its wild type counterpart, the kappaI O18/O8 light chain germline. Crystallographic studies indicate that both proteins form dimers. However, AL-09 has an altered dimer interface that is rotated 90 masculine from the kappaI O18/O8 dimer interface. The three non-conservative mutations in AL-09 are located within the dimer interface, consistent with their role in the decreased stability of this amyloidogenic protein. Moreover, AL-09 forms amyloid fibrils more quickly than kappaI O18/O8 in vitro. These results support the notion that the increased stability of the monomer and delayed fibril formation, together with a properly formed dimer, may be protective against amyloidogenesis. This could open a new direction into rational drug design for amyloidogenic proteins.
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<div class="pdbe-citations 2q1e" style="background-color:#fffaf0;"></div>
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== References ==
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==About this Structure==
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<references/>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q1E OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Homo sapiens]]
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Altered dimer interface decreases stability in an amyloidogenic protein., Baden EM, Owen BA, Peterson FC, Volkman BF, Ramirez-Alvarado M, Thompson JR, J Biol Chem. 2008 Apr 8;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18400753 18400753]
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[[Category: Large Structures]]
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[[Category: Baden, E M.]]
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[[Category: Baden EM]]
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[[Category: Ramirez-Alvarado, M.]]
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[[Category: Ramirez-Alvarado M]]
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[[Category: Thompson, J R.]]
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[[Category: Thompson JR]]
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[[Category: Al]]
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[[Category: Amyloid]]
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[[Category: Immunoglobulin]]
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[[Category: Light chain]]
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[[Category: Light chain amyloidosis]]
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[[Category: Light chain variable domain]]
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[[Category: Protein fibril]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:27:10 2008''
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Current revision

Altered dimer interface decreases stability in an amyloidogenic kappa1 Bence Jones protein.

PDB ID 2q1e

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