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Cover Image, Volume 107, Issue 8
Publication year - 2017
Publication title -
biopolymers
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22955
Subject(s) - chemistry , mutant , citation , immunoglobulin light chain , computational biology , computer science , antibody , information retrieval , stereochemistry , biochemistry , world wide web , genetics , biology , gene
Light chain amyloidosis is a misfolding disease characterized by the polymerization of immunoglobulins as amyloid fibers. Lambda 6a Ig light chain domains are highly frequent among patients with this disorder. Valdés‐García et al . describe how the mutants R24G (red backbone) and P7S (green backbone) push the germline protein (blue backbone) into an amyloidogenic pathway through a convergent mechanism. Both mutations, despite being at different locations, promote the dislodgment of the same anti‐aggregation motif. The results point to the beginning of an amyloidogenic pathway and may be helpful when designing drugs to stabilize the native‐like folded state. (DOI: 10.1002/bip.23027 )

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