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(1)H, (15)N and (13)C resonance assignments for 3rC and 3rCWP: amyloidogenic variants of imunoglobulin λ 3 light-chain.
MedLine Citation:
PMID:  24816896     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Primary amyloidosis (AL) is the most common amyloid systemic disease and it is characterized by the deposition of immunoglobulin light-chain amyloid fibers in different organs, causing organ failure. The germ-line lambda 3 immunoglobulin light-chain proteins have been correlated with the AL condition. Two mutants have been derived from this germ-line, the single mutant C34Y (3rC) and the triple mutant C34Y, W35A and P7D (3rCWP), presenting a remarkable difference in amyloid fibril formation propensities in vitro. Here we report the (1)H, (13)C and (15)N resonance assignments of these proteins, as the first step to use solution nuclear magnetic resonance spectroscopy to get a better understanding of the amyloid fibril formation differences between these two mutants.
Authors:
Paloma Gil-Rodríguez; Carlos Amero
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-5-11
Journal Detail:
Title:  Biomolecular NMR assignments     Volume:  -     ISSN:  1874-270X     ISO Abbreviation:  Biomol NMR Assign     Publication Date:  2014 May 
Date Detail:
Created Date:  2014-5-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101472371     Medline TA:  Biomol NMR Assign     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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